+

WO2001019999A1 - Gene codant une nouvelle threonyl-arnt synthase, ses utilisations et procedes de preparation - Google Patents

Gene codant une nouvelle threonyl-arnt synthase, ses utilisations et procedes de preparation Download PDF

Info

Publication number
WO2001019999A1
WO2001019999A1 PCT/CN2000/000275 CN0000275W WO0119999A1 WO 2001019999 A1 WO2001019999 A1 WO 2001019999A1 CN 0000275 W CN0000275 W CN 0000275W WO 0119999 A1 WO0119999 A1 WO 0119999A1
Authority
WO
WIPO (PCT)
Prior art keywords
polypeptide
ribonucleic acid
polynucleotide
sequence
threonyl
Prior art date
Application number
PCT/CN2000/000275
Other languages
English (en)
Chinese (zh)
Inventor
Yumin Mao
Yi Xie
Original Assignee
Shanghai Biorigin Gene Development Co. Ltd.
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Shanghai Biorigin Gene Development Co. Ltd. filed Critical Shanghai Biorigin Gene Development Co. Ltd.
Priority to CN00812873A priority Critical patent/CN1375007A/zh
Publication of WO2001019999A1 publication Critical patent/WO2001019999A1/fr

Links

Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/93—Ligases (6)
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
    • Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
    • Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
    • Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change

Definitions

  • the present invention relates to a polynucleotide sequence encoding a novel human threonyl transfer ribonucleic acid synthetase.
  • the present invention also relates to a method for preparing the polynucleotide and a protein encoded by the same, and the polynucleotide and the encoding Use of protein. Background of the invention
  • Aminoacyltransferases are a large family of enzymes. In prokaryotes there are at least twenty different forms of amino acid aminoamidine transfer ribonucleic acid synthetases, while in eukaryotes there are only two forms. Amino acid aminoacyltransferase synthetase, namely: cytosolic and mitochondrial type, they have a common quaternary structure, and their subunits have multiple changes [Schimmd P. Annu. Rev. Biochem.) 56: 125-158 (1987)].
  • Aminoacyltransferase synthetases can be divided into two groups: Group I consists mainly of kinases and dehydrogenases, and the remaining synthetases are grouped into Group II.
  • the II enzyme has three characteristic sequence motifs, motif 1 is the dimer interface, and motifs 2 and 3 are active sites. When the amino acid and ATP binding sites undergo a contact reaction, the II enzyme is combined into an enzyme. This results in a structural fold, which is different from the Rossmann fold pattern of group I.
  • the second group of alcohols can be further subdivided into groups 2a (proline, threonine, histidine, serine, etc.) and group 2b (aspartic acid, aspartyl, and lysine, etc.) ),
  • groups 2a proline, threonine, histidine, serine, etc.
  • group 2b aspartic acid, aspartyl, and lysine, etc.
  • Both sets of aminoacyltransferase synthetases can activate amino acids.
  • the activated amino acids are transferred to specific tRNA molecules, but they are attached to ATP.
  • Different sites Group I enzymes are attached to 2, hydroxyl groups, and group II enzymes are attached to 3, hydroxyl groups [Eriani G. et al., J Mol Evol. 1995 40 (5): 499- 508] .
  • Threonyltransferase synthetase (hereinafter abbreviated as thrS) is one of the members of the large family of aminotransferase synthetases, and it has the structure and function of the aforementioned aminoacyltransferase synthesis.
  • Human threonyl transferase synthase and threonine transfer ribonucleic acid synthase found in cytoplasm, yeast mitochondria, and B. subtilis have high homology. A detailed understanding of threonyl transfer ribonucleic acid synthase and its signal transduction pathways of S.
  • aureus has revealed some mechanisms of inflammatory diseases and uncontrolled proliferative diseases [Hodgson, et al., U.S. Patent, 5795757].
  • the human threonyl transfer ribonucleic acid synthetase cDNA, oligonucleotides, peptides, and antibodies thereof provided by the present invention are useful for studying signal transduction in different tissues and cells, and for diagnosing diseases related to threonine transfer ribonucleic acid synthase disorders It is of great value to classify threonine transfer ribonuclease synthetase inhibitors or drugs used to treat these diseases. Summary of invention
  • Another object of the present invention is to provide a polynucleotide sequence encoding a threonine transfer ribonucleic acid synthetase.
  • Another object of the present invention is to provide a recombinant expression vector containing a polynucleotide encoding a threonine transfer ribonucleic acid synthetase.
  • Another object of the present invention is to provide a host cell comprising a recombinant expression vector having a polynucleotide encoding a threonyl transfer ribonucleic acid-synthesizing alcohol.
  • Another object of the invention is to provide antagonists against the polypeptides of the invention.
  • Another object of the present invention is to provide a method for diagnosing and treating diseases related to abnormal function of threonyl transferase synthetase.
  • the present invention provides a substantially pure threonyl transfer ribonucleic acid synthetase consisting essentially of the amino acid sequence shown in SEQ ID NO: 2. Threonyl transfer ribonucleic acid synthesis is characterized by having a glutamyl transfer ribonucleic acid synthetase domain.
  • substantially pure is threonine transfer ribonucleic acid synthesizer which is essentially free of other proteins, lipids, carbohydrates or other substances with which it is naturally associated.
  • Those skilled in the art can purify threonine transfer ribonucleic acid synthetase using standard protein purification techniques.
  • Substantially pure peptides can produce a single main band on a non-reducing polyacrylamide gel.
  • the purity of threonine transfer RNA synthetase can be analyzed by amino acid sequence.
  • the polypeptide of the present invention may be a recombinant polypeptide, a natural polypeptide, or a synthetic polypeptide, and preferably a recombinant polypeptide.
  • the invention also includes fragments, derivatives and analogs of the polypeptide.
  • fragment refers to a polypeptide that substantially maintains the same biological function or activity of the polypeptide according to the present invention.
  • the polypeptide of the present invention such as a fragment, derivative or analog of SEQ ID NO: 2 may be: (I) a polypeptide in which one or more amino acid residues Group is substituted by a conservative or non-conservative amino acid residue (preferably a conservative amino acid residue), and the substituted amino acid may or may not be encoded by a genetic codon; or (II) a polypeptide in which one or more amino acids The residue contains a substituent; or
  • the invention provides an isolated polynucleotide consisting essentially of a polynucleotide encoding a polypeptide having the amino acid sequence of SEQ ID NO: 2.
  • the polynucleotide sequence of the present invention includes the nucleotide sequence of SEQ ID NO: 1.
  • the polynucleotide of the present invention is found from a cDNA library of human fetal brain tissue. It contains a polynucleotide sequence of 2741 bases in length and its open reading frame encodes 718 amino acids. According to the amino acid sequence homology comparison, it was found that this polypeptide has 61% homology with thrS in yeast mitochondria, and the polypeptide has conserved bases in the thrS gene family, which can be inferred from the synthesis of this new human threonyl transfer ribonucleic acid The enzyme has a similar structure and function of the thrS gene family.
  • isolated refers to the separation of a substance from its original environment (if it is a natural substance, the original environment is the natural environment).
  • polynucleotides and polypeptides in a natural state in a living cell are not isolated and purified, but the same polynucleotides or polypeptides are separated and purified if they are separated from other substances existing in the natural state.
  • the polynucleotide of the present invention may be in the form of DNA or RNA.
  • DNA forms include cDNA, genomic DNA, or synthetic DNA.
  • DNA can be single-stranded or double-stranded.
  • DNA can be coding or non-coding.
  • the coding region sequence encoding a mature polypeptide may be the same as the coding region sequence shown in SEQ ID NO: 1 or a degenerate variant.
  • a "degenerate variant" is It refers to a nucleic acid sequence that encodes a protein or peptide having SEQ ID NO: 2, but is different from the coding region sequence shown in SEQ ID NO: 1 due to the coexistence of codons.
  • the polynucleotide encoding the mature polypeptide of SEQ ID NO: 2 includes: only the coding sequence of the mature polypeptide; the coding sequence of the mature polypeptide and various additional coding sequences; the coding sequence of the mature polypeptide (and optional additional coding sequences); and Non-coding sequence.
  • polynucleotide encoding a polypeptide refers to a polynucleotide comprising a polynucleotide encoding the polypeptide and a polynucleotide comprising additional coding and / or non-coding sequences.
  • the invention also relates to variants of the polynucleotides described above, which encode polypeptides or fragments, analogs and derivatives of polypeptides having the same amino acid sequence as the invention.
  • This variant of the polynucleotide may be a naturally occurring allelic variant or a non-naturally occurring variant.
  • These nucleotide variants include substitution variants, deletion variants, and insertion variants.
  • an allelic variant is an alternative form of a polynucleotide, which may be a substitution, deletion, or insertion of one or more nucleotides, but does not substantially alter the function of the polypeptide it encodes.
  • the invention also relates to a polynucleotide capable of hybridizing to the sequence described above (there is at least 70%, preferably 80%, more preferably 90%, or 95% identity between the two sequences).
  • the present invention particularly relates to polynucleotides that can hybridize to the polynucleotides of the present invention under stringent conditions.
  • “strict conditions” means: (1) hybridization and elution at lower ionic strength and higher temperature, such as 0.2xSSC, 0.1% SDS, 60 "; or (2) added during hybridization Denaturing agents, such as 50% (v / v) formamidine, 0.1% calf serum / 0.1% Ficoll, 42, etc .; or (3) only the identity between the two sequences is at least 95% or better, preferably Hybridization occurs only when it is above 97%.
  • the polypeptide encoded by the hybridizable polynucleotide has the same biological function and activity as the mature polypeptide shown in SEQ ID NO: 2.
  • nucleic acid fragments that hybridize to the sequences described above.
  • a "nucleic acid fragment” is at least 15 nucleotides in length, preferably at least 15 nucleotides in length. 20-30 nucleotides, more preferably at least 50-60 nucleotides, and most preferably at least 100 nucleotides.
  • Nucleic acid fragments can be used in nucleic acid amplification techniques, such as PCR, to identify and / or isolate polynucleotides encoding threonyl transfer ribonucleic acid synthetase.
  • the present invention also relates to a vector comprising a polynucleotide sequence of the present invention, a host cell produced by a genetic engineering method using the vector of the present invention, and a method for producing a polypeptide according to the present invention by recombinant technology.
  • DNA sequence of the present invention can be obtained by several methods.
  • DNA is isolated using hybridization techniques known in the art. These techniques include, but are not limited to: 1) hybridization of probes to genomic or cDNA libraries to detect homologous nucleotide sequences, and 2) antibody screening of expression libraries to detect cloned DNA fragments that share common structural features .
  • DNA fragment sequences encoding threonyltransferases can also be obtained by: 1) isolating double-stranded DNA sequences from genomic DNA; 2) chemically synthesizing DNA sequences to obtain double-stranded DNA of the desired polypeptide-as described above
  • genomic DNA isolation is the most commonly used.
  • direct chemical synthesis of the DNA sequence is also an alternative method. If the entire sequence of the required number of amino acids is unclear, direct chemical synthesis of the DNA sequence is not possible, and the method chosen is the isolation of the cDNA sequence.
  • the standard method for isolating the cDNA of interest is to isolate mRNA from donor cells that overexpress the gene and perform reverse transcription to form a scutellum or phage cDNA library.
  • mRNA mRNA from donor cells that overexpress the gene and perform reverse transcription to form a scutellum or phage cDNA library.
  • kits are also commercially available (Qiagene).
  • the construction of cDNA libraries is also a common method (Sambrook et al., Molecular Cloning, a Laboratory Manual, Cold Spring Harbor Laboratory. New York, 1989).
  • Commercially available cDNA libraries are also available, such as different cDNA libraries from Clontech. When combined with polymerase chain reaction technology, even very small expression products can be cloned. These genes can be screened from these cDNA libraries by conventional methods.
  • These methods include (but are not limited to): (1) DNA-DNA or DNA-RNA hybridization; (2) the presence or loss of function of a marker gene; (3) determination of the level of a threonyl transfer ribonucleic acid-synthesized transcript (4) applying immunological techniques or measuring biological activity to detect the protein product of gene expression.
  • the above methods can be used singly or in combination.
  • the probe used for hybridization is a nucleotide sequence that is homologous to any part of the polynucleotide of the present invention, and has a length of at least 15 nucleotides, preferably 20-30 nuclei.
  • the nucleotide is preferably 50 to 60 nucleotides, and more preferably 100 nucleotides or more.
  • the probe used here is usually a DNA sequence chemically synthesized based on the DNA sequence information of the gene of the present invention.
  • the gene itself or a fragment of the present invention can of course be used as a probe.
  • DNA probes can be labeled with radioisotopes, luciferin, or enzymes (such as alkaline phosphatase).
  • immunological techniques such as Western blotting, radioimmunoprecipitation, and enzyme-linked immunosorbent assay (ELISA) can be used to detect the protein product expressed by the threonyltransferase synthetase gene expression.
  • ELISA enzyme-linked immunosorbent assay
  • the method of using the PCR technique to amplify DNA / RNA can be preferentially used to obtain the gene of the present invention.
  • the RACE method RACE: Rapid Amplification of cDNA Ends
  • the primers used in the above PCR can be appropriately based on the sequence information of the invention disclosed herein Select and synthesize using conventional methods.
  • the amplified DNA / RNA fragments can be isolated and purified by conventional methods such as by gel electrophoresis.
  • nucleotide sequence of the gene of the present invention or various DNA fragments and the like obtained as described above can be measured by a conventional method such as dideoxy chain termination method (Sanger et al. PNAS, 1977, 74: 5463-5467). This type of nucleotide sequence determination is also available Industry sequencing kits. In order to obtain the full-length cDNA sequence, sequencing must be repeated. Sometimes it is necessary to determine the cDNA sequence of multiple clones in order to splice into a full-length cDNA sequence.
  • the polynucleotide sequence of the present invention can be used to express or produce recombinant threonine transfer ribonucleic acid synthetase (Science, 1984; 224: 1431). Generally there are the following steps:
  • the threonine transfer ribonucleic acid synthetase polynucleotide sequence can be inserted into a recombinant expression vector.
  • recombinant expression vector refers to bacterial plasmids, phages, yeast plasmids, plant cell viruses, mammalian cell viruses such as adenoviruses, retroviruses, or other vectors that are well known in the art.
  • Vectors suitable for use in the present invention include, but are not limited to: T7-based expression vectors (Rosenberg, et al., Gene, 1987, 56: 125) expressed in bacteria; pMSX D expression vectors (Lee) expressed in mammalian cells And Nathans, Journal of Biochemistry, 263: 3521, 1988) and baculovirus-derived vectors expressed in insect cells.
  • T7-based expression vectors Rosenberg, et al., Gene, 1987, 56: 125
  • pMSX D expression vectors Lee expressed in mammalian cells And Nathans, Journal of Biochemistry, 263: 3521, 1988
  • baculovirus-derived vectors expressed in insect cells baculovirus-derived vectors expressed in insect cells.
  • any plasmid and vector can be used as long as it can be replicated and stabilized in the host.
  • An important feature of expression vectors is that they usually contain origins of replication, promoters, marker genes and translation control elements.
  • Methods known to those skilled in the art can be used to construct an expression vector containing a threonyltransferase synthetase-encoding DNA sequence and appropriate transcription / translation control signals. These methods include in vitro recombinant DNA technology, DNA synthesis technology, and in vivo recombination technology (Sambroook, et al., Molecular Cloning, a laboratory Manual, cold Spring Harbor laboraty. New York, 1989). Said The DNA sequence is operably linked to an appropriate promoter in the expression vector to direct mRNA synthesis. Representative examples of these promoters are: E.
  • the expression vector also includes a ribosome binding site for translation initiation and a transcription terminator.
  • the expression vector preferably contains one or more selectable marker genes to provide phenotypic traits for the selection of transformed host cells, such as dihydrofolate reductol for use in eukaryotic cell culture, neomycin resistance, and Green fluorescent protein (GFP), or tetracycline or ampicillin resistance for E. coli.
  • selectable marker genes to provide phenotypic traits for the selection of transformed host cells, such as dihydrofolate reductol for use in eukaryotic cell culture, neomycin resistance, and Green fluorescent protein (GFP), or tetracycline or ampicillin resistance for E. coli.
  • Vectors containing the appropriate DNA sequences and appropriate promoters or control sequences described above can be used to transform appropriate host cells so that they can express proteins.
  • the host cell can be a prokaryotic cell, such as a bacterial cell; or a lower eukaryotic cell, such as a yeast cell; or a higher eukaryotic cell, such as a mammalian cell.
  • a prokaryotic cell such as a bacterial cell
  • a lower eukaryotic cell such as a yeast cell
  • a higher eukaryotic cell such as a mammalian cell.
  • Representative examples are: E. coli, Streptomyces; bacterial cells of Salmonella typhimurium; fungal cells such as yeast; plant cells; insect cells of Drosophila S2 or Sf9; animals of CHO, COS or Bowes melanoma cells Cells etc.
  • Enhancers are cis-acting factors of DNA, usually about 10 to 300 base pairs, that act on promoters to enhance gene transcription.
  • Illustrative examples include SV40 enhancers of 100 to 270 base pairs on the late side of the origin of replication, polyoma enhancers on the late side of the origin of replication, and adenoviral enhancers.
  • Transformation of host cells with recombinant DNA can be performed using conventional techniques well known to those skilled in the art.
  • the host is a prokaryote, such as E. coli
  • the preparation of competent cells capable of absorbing DNA is generally harvested from the exponential growth phase and treated with the CaCl 2 method. The steps used are well known in the art. Alternatively, MgCl 2 is used. If necessary, transformation can also be performed by electroporation.
  • the host is a eukaryote, the following DNA transfection methods can be used: calcium gallate co-precipitation method, conventional mechanical methods such as obvious sign injection, electroporation, and liposome packaging.
  • the recombinant polypeptide required in the above method is coated intracellularly, extracellularly, or expressed on the cell membrane or secreted extracellularly.
  • the physical, chemical, and other properties can be used to isolate and purify the recombinant protein by various separation methods. These methods are well known to those skilled in the art. More specifically, conventional renaturation, treatment with a protein precipitant (salting out method), centrifugation, osmotic lysis, ultra-treatment, ultra-centrifugation, molecular sieve chromatography (gel filtration), and adsorption chromatography can be mentioned. , Ion exchange chromatography, high performance liquid chromatography (HPLC) and various other liquid chromatography techniques and combinations of these methods.
  • antibodies against threonine transfer ribonucleic acid synthase epitopes include, but are not limited to, polyclonal antibodies, monoclonal antibodies, chimeric antibodies, single chain antibodies, Fab fragments, and fragments produced by Fab expression libraries.
  • Antibodies against threonyltransferase synthetase can be used in immunohistochemical techniques to detect threonyltransferase synthetase in biopsy specimens.
  • Antibodies can also be used to design immunotoxins that target a particular part of the body.
  • threonyltransferase synthetase-rich monoclonal antibodies can covalently bind to bacterial or phytotoxins (such as diphtheria toxin, ricin, ormosine, etc.).
  • a common method is to attack the amino group of the antibody with a thiol cross-linking agent such as SPDP and bind the toxin to the antibody through the exchange of disulfide bonds.
  • This hybrid antibody can be used to kill threonyl transfer ribonucleic acid synthase Cell.
  • the invention also relates to a diagnostic test method for quantitative and qualitative detection of threonine transfer ribonucleic acid synthase levels.
  • tests are well known in the art and include FLISH assays and radioimmunoassays.
  • the level of threonyltransferase synthetase detected in the test can be used to explain the importance of threonine transfer ribonucleic acid synthetase in various diseases, and to diagnose the role of threonyltransferase synthetase. disease.
  • a polynucleotide sequence encoding a threonine transfer ribonucleic acid synthetase can be used to hybridize biopsy specimens to determine abnormal expression of threonyl transfer ribonucleic acid synthesis.
  • Hybridization techniques include Southern blotting, Northern blotting, in situ hybridization, and the like. These techniques and methods are publicly available and mature, and related kits are commercially available.
  • a part or all of the polynucleotide of the present invention can be used as a probe to be fixed on a microarray (Microarray) or a DNA chip (DNA Chip) for analyzing differential expression analysis and gene diagnosis of genes in a tissue.
  • Tranylase synthetase-specific primers for RNA-polymerase chain reaction (RT-PCR) amplification in vitro can also detect the transcription product of threonyltransferase synthetase.
  • Ndel and Hindlll digestion sites respectively, followed by the coding sequences of the target gene 3, 5 and 5, respectively, using the pBS plasmid containing the full-length target gene as a template for the PCR reaction.
  • the restriction sites of Ndel and Hindlll correspond to the selective endonuclease sites on the expression vector plasmid PTSA-18.
  • Ndel and Hindlll were used to digest and ligate the amplified sequence and plasmid PTSA-18, respectively.
  • the recombinant plasmid was transformed into the host strain E. coli BL21 (DE3) plySs, and induced by IPTG for expression.
  • the expressed product was sonicated and heat-denatured, and then applied to a DEAE column to obtain a purified target protein.
  • Example 3 Homologous search of cDNA clones
  • the novel human threonyl transfer ribonucleic acid synthetase protein polynucleotide sequence provided by the present invention and its encoded protein sequence are used to perform homology search in databases such as Genbank and Swissport.
  • the program for searching is called Blast (Basic local Alignment search tool) (1993 Proc Nat Acad Sci 90: 5873- 5877), Blast can find many genes that are homologous to threonyl transfer ribonucleic acid synthetase protein, among which the gene with the most homology to the gene we invented, Its encoded protein has the accession number M63180 in Genbank. These retrieved genes or protein sequences can be retrieved from the Genbank database.
  • the recalled sequences can be compared using the Pileup (multi-sequence) and Gap (two-sequence) programs in the GCG software package. Functional prediction of new proteins can be analyzed using the Motif program.
  • the results of the homology search are shown below. The results show that the human threonyl transfer ribonucleic acid synthetase protein provided by the present invention has 61% homology with the human threonyl transfer ribonucleic acid synthetase protein provided in the Genband database ( (See the table below for details). -61-
  • Example 4 Production of anti-threonyl transfer ribonuclease synthetase antibody
  • the following threonyl transfer ribonucleic acid-synthetic peptide was synthesized using a peptide synthesizer (PE-ABI): H2-Leu Tyr Gin Arg Trp Arg Cys Leu Arg Leu-COOH.
  • the polypeptide is coupled to hemocyanin and bovine serum albumin to form a complex, respectively.
  • Rabbits were immunized with 4 mg of the hemocyanin polypeptide complex plus complete Freund's adjuvant, and 15 days later, the hemocyanin polypeptide complex plus incomplete Freund's adjuvant was used to boost immunity once.
  • a titer plate coated with a 15 ⁇ 8 / ⁇ 1 bovine serum albumin peptide complex was used as an ELISA to determine the antibody titer in rabbit serum.
  • Total Ig G was isolated from antibody-positive rabbit serum using protein A-Sepharose.
  • the peptide was bound to a cyanogen bromide-activated Sepharose 4B column, and the anti-peptide antibody was separated from the total IgG by affinity chromatography.
  • the immunoprecipitation method proved that the purified antibody could specifically bind to threonyltransferase synthetase.
  • Trp Asn Thr Thr Pro Tyr Gin Leu Ala Arg Gin lie Ser Ser Thr

Landscapes

  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Organic Chemistry (AREA)
  • Zoology (AREA)
  • Engineering & Computer Science (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Wood Science & Technology (AREA)
  • Microbiology (AREA)
  • Biotechnology (AREA)
  • Biomedical Technology (AREA)
  • Molecular Biology (AREA)
  • Biochemistry (AREA)
  • General Engineering & Computer Science (AREA)
  • General Health & Medical Sciences (AREA)
  • Medicinal Chemistry (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)
  • Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)

Abstract

La présente invention se rapporte à une séquence polynucléotidique codant une nouvelle thréonyl-ARNt synthase humaine. Elle se rapporte également aux procédés de préparation de ce polynucléotide et à la protéine qu'il code selon une technique de recombinaison. L'invention se rapporte également aux utilisations de cette thréonyl-ARNt synthase et de la séquence polynucléotidique codant ledit polypeptide pour la préparation d'une composition pharmaceutique destinée au traitement de maladies associées à une activité faible ou nulle de la thréonyl-ARNt synthase humaine, et notamment au traitement de diverses tumeurs. Cette invention se rapporte également à des procédés de préparation d'anticorps dirigés contre ledit polypeptide, à des agonistes de dépistage ainsi qu'à leurs utilisations thérapeutiques.
PCT/CN2000/000275 1999-09-14 2000-09-14 Gene codant une nouvelle threonyl-arnt synthase, ses utilisations et procedes de preparation WO2001019999A1 (fr)

Priority Applications (1)

Application Number Priority Date Filing Date Title
CN00812873A CN1375007A (zh) 1999-09-14 2000-09-14 编码一种新的苏氨酰转移核糖核酸合成酶的基因及其应用和制备方法

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
CN99116872 1999-09-14
CN99116872.0 1999-09-14

Publications (1)

Publication Number Publication Date
WO2001019999A1 true WO2001019999A1 (fr) 2001-03-22

Family

ID=5279542

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/CN2000/000275 WO2001019999A1 (fr) 1999-09-14 2000-09-14 Gene codant une nouvelle threonyl-arnt synthase, ses utilisations et procedes de preparation

Country Status (1)

Country Link
WO (1) WO2001019999A1 (fr)

Cited By (28)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP2563382A2 (fr) * 2010-04-27 2013-03-06 aTyr Pharma, Inc. Découverte innovante de compositions thérapeutiques, de diagnostic et d'anticorps se rapportant à des fragments protéiques de thréonyl arnt synthétases
US8946157B2 (en) 2010-05-03 2015-02-03 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of seryl-tRNA synthetases
US8945541B2 (en) 2010-05-14 2015-02-03 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of phenylalanyl-beta-tRNA synthetases
US8961961B2 (en) 2010-05-03 2015-02-24 a Tyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related protein fragments of arginyl-tRNA synthetases
US8962560B2 (en) 2010-06-01 2015-02-24 Atyr Pharma Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of Lysyl-tRNA synthetases
US8961960B2 (en) 2010-04-27 2015-02-24 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of isoleucyl tRNA synthetases
US8969301B2 (en) 2010-07-12 2015-03-03 Atyr Pharma Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of aspartyl-tRNA synthetases
US8981045B2 (en) 2010-05-03 2015-03-17 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of methionyl-tRNA synthetases
US8980253B2 (en) 2010-04-26 2015-03-17 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of cysteinyl-tRNA synthetase
US8986680B2 (en) 2010-04-29 2015-03-24 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of Asparaginyl tRNA synthetases
US8993723B2 (en) 2010-04-28 2015-03-31 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of alanyl-tRNA synthetases
US8999321B2 (en) 2010-07-12 2015-04-07 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of glycyl-tRNA synthetases
US9029506B2 (en) 2010-08-25 2015-05-12 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of tyrosyl-tRNA synthetases
US9034321B2 (en) 2010-05-03 2015-05-19 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of phenylalanyl-alpha-tRNA synthetases
US9034598B2 (en) 2010-05-17 2015-05-19 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of leucyl-tRNA synthetases
US9034320B2 (en) 2010-04-29 2015-05-19 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of Valyl-tRNA synthetases
US9062301B2 (en) 2010-05-04 2015-06-23 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of glutamyl-prolyl-tRNA synthetases
US9062302B2 (en) 2010-05-04 2015-06-23 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of p38 multi-tRNA synthetase complex
US9068177B2 (en) 2010-04-29 2015-06-30 Atyr Pharma, Inc Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of glutaminyl-tRNA synthetases
US9399770B2 (en) 2010-10-06 2016-07-26 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of tryptophanyl-tRNA synthetases
US9422539B2 (en) 2010-07-12 2016-08-23 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of histidyl-tRNA synthetases
US9587235B2 (en) 2013-03-15 2017-03-07 Atyr Pharma, Inc. Histidyl-tRNA synthetase-Fc conjugates
US9688978B2 (en) 2011-12-29 2017-06-27 Atyr Pharma, Inc. Aspartyl-tRNA synthetase-Fc conjugates
US9714419B2 (en) 2011-08-09 2017-07-25 Atyr Pharma, Inc. PEGylated tyrosyl-tRNA synthetase polypeptides
US9796972B2 (en) 2010-07-12 2017-10-24 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of glycyl-tRNA synthetases
US9816084B2 (en) 2011-12-06 2017-11-14 Atyr Pharma, Inc. Aspartyl-tRNA synthetases
US9822353B2 (en) 2011-12-06 2017-11-21 Atyr Pharma, Inc. PEGylated aspartyl-tRNA synthetase polypeptides
US11767520B2 (en) 2017-04-20 2023-09-26 Atyr Pharma, Inc. Compositions and methods for treating lung inflammation

Non-Patent Citations (4)

* Cited by examiner, † Cited by third party
Title
DATABASE GENBANK [online] 10 July 1999 (1999-07-10), Database accession no. AC004987 *
DATABASE GENBANK [online] 10 September 1999 (1999-09-10), Database accession no. AC008134 *
DATABASE GENBANK [online] 19 July 1999 (1999-07-19), Database accession no. AF111169 *
DATABASE GENBANK [online] 30 October 1998 (1998-10-30), Database accession no. AC002036 *

Cited By (67)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US8980253B2 (en) 2010-04-26 2015-03-17 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of cysteinyl-tRNA synthetase
US10717786B2 (en) 2010-04-26 2020-07-21 aTye Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of Cysteinyl-tRNA synthetase
US10030077B2 (en) 2010-04-26 2018-07-24 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of cysteinyl-tRNA synthetase
US9540629B2 (en) 2010-04-26 2017-01-10 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of Cysteinyl-tRNA synthetase
US9896515B2 (en) 2010-04-27 2018-02-20 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of isoleucyl tRNA synthetases
US9528103B2 (en) 2010-04-27 2016-12-27 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of isoleucyl tRNA synthetases
US8961960B2 (en) 2010-04-27 2015-02-24 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of isoleucyl tRNA synthetases
EP2563382A4 (fr) * 2010-04-27 2013-11-20 Atyr Pharma Inc Découverte innovante de compositions thérapeutiques, de diagnostic et d'anticorps se rapportant à des fragments protéiques de thréonyl arnt synthétases
US9580706B2 (en) 2010-04-27 2017-02-28 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of threonyl-tRNA synthetases
EP2563382A2 (fr) * 2010-04-27 2013-03-06 aTyr Pharma, Inc. Découverte innovante de compositions thérapeutiques, de diagnostic et d'anticorps se rapportant à des fragments protéiques de thréonyl arnt synthétases
US8986681B2 (en) 2010-04-27 2015-03-24 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of threonyl-tRNA synthetases
US10563192B2 (en) 2010-04-27 2020-02-18 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of threonyl-tRNA synthetases
US10150958B2 (en) 2010-04-27 2018-12-11 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of threonyl-tRNA synthetases
US9320782B2 (en) 2010-04-28 2016-04-26 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of alanyl tRNA synthetases
US8993723B2 (en) 2010-04-28 2015-03-31 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of alanyl-tRNA synthetases
US9034320B2 (en) 2010-04-29 2015-05-19 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of Valyl-tRNA synthetases
US8986680B2 (en) 2010-04-29 2015-03-24 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of Asparaginyl tRNA synthetases
US9556425B2 (en) 2010-04-29 2017-01-31 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of Valyl-tRNA synthetases
US10189911B2 (en) 2010-04-29 2019-01-29 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of Valyl-tRNA synthetases
US9623093B2 (en) 2010-04-29 2017-04-18 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of asparaginyl tRNA synthetases
US9068177B2 (en) 2010-04-29 2015-06-30 Atyr Pharma, Inc Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of glutaminyl-tRNA synthetases
US8961961B2 (en) 2010-05-03 2015-02-24 a Tyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related protein fragments of arginyl-tRNA synthetases
US10179906B2 (en) 2010-05-03 2019-01-15 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of phenylalanyl-alpha-tRNA synthetases
US8946157B2 (en) 2010-05-03 2015-02-03 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of seryl-tRNA synthetases
US9340780B2 (en) 2010-05-03 2016-05-17 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of seryl-tRNA synthetases
US8981045B2 (en) 2010-05-03 2015-03-17 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of methionyl-tRNA synthetases
US9593322B2 (en) 2010-05-03 2017-03-14 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of arginyl-trna synthetases
US9593323B2 (en) 2010-05-03 2017-03-14 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of phenylalanyl-alpha-tRNA synthetases
US9034321B2 (en) 2010-05-03 2015-05-19 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of phenylalanyl-alpha-tRNA synthetases
US9422538B2 (en) 2010-05-03 2016-08-23 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of methionyl-tRNA synthetasis
US9062302B2 (en) 2010-05-04 2015-06-23 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of p38 multi-tRNA synthetase complex
US10160814B2 (en) 2010-05-04 2018-12-25 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of glutamyl-prolyl-tRNA synthetases
US9062301B2 (en) 2010-05-04 2015-06-23 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of glutamyl-prolyl-tRNA synthetases
US9404104B2 (en) 2010-05-04 2016-08-02 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of P38 multi-tRNA synthetase complex
US9574187B2 (en) 2010-05-04 2017-02-21 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of glutamyl-prolyl-tRNA synthetases
US8945541B2 (en) 2010-05-14 2015-02-03 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of phenylalanyl-beta-tRNA synthetases
US10220080B2 (en) 2010-05-14 2019-03-05 aTyr Pharam, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of phenylalanyl-beta-tRNA synthetases
US9687533B2 (en) 2010-05-14 2017-06-27 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of phenylalanyl-beta-tRNA synthetases
US10179908B2 (en) 2010-05-17 2019-01-15 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of leucyl-tRNA synthetases
US9790482B2 (en) 2010-05-17 2017-10-17 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of leucyl-tRNA synthetases
US9034598B2 (en) 2010-05-17 2015-05-19 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of leucyl-tRNA synthetases
US9347053B2 (en) 2010-05-27 2016-05-24 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of glutaminyl-tRNA synthetases
US9322009B2 (en) 2010-06-01 2016-04-26 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of Lysyl-tRNA synthetases
US8962560B2 (en) 2010-06-01 2015-02-24 Atyr Pharma Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of Lysyl-tRNA synthetases
US9637730B2 (en) 2010-07-12 2017-05-02 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of histidyl-tRNA synthetases
US9796972B2 (en) 2010-07-12 2017-10-24 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of glycyl-tRNA synthetases
US8969301B2 (en) 2010-07-12 2015-03-03 Atyr Pharma Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of aspartyl-tRNA synthetases
US10669533B2 (en) 2010-07-12 2020-06-02 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of Histidyl-tRNA synthetases
US9315794B2 (en) 2010-07-12 2016-04-19 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of aspartyl-tRNA synthetases
US8999321B2 (en) 2010-07-12 2015-04-07 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of glycyl-tRNA synthetases
US9422539B2 (en) 2010-07-12 2016-08-23 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of histidyl-tRNA synthetases
US10196628B2 (en) 2010-07-12 2019-02-05 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of histidyl-tRNA synthetases
US10196629B2 (en) 2010-07-12 2019-02-05 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of glycyl-tRNA synthetases
US9029506B2 (en) 2010-08-25 2015-05-12 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of tyrosyl-tRNA synthetases
US9428743B2 (en) 2010-08-25 2016-08-30 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of tyrosyl-trna synthetases
US10563191B2 (en) 2010-10-06 2020-02-18 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related protein fragments of tryptophanyl tRNA synthetases
US9399770B2 (en) 2010-10-06 2016-07-26 Atyr Pharma, Inc. Innovative discovery of therapeutic, diagnostic, and antibody compositions related to protein fragments of tryptophanyl-tRNA synthetases
US9714419B2 (en) 2011-08-09 2017-07-25 Atyr Pharma, Inc. PEGylated tyrosyl-tRNA synthetase polypeptides
US9816084B2 (en) 2011-12-06 2017-11-14 Atyr Pharma, Inc. Aspartyl-tRNA synthetases
US9822353B2 (en) 2011-12-06 2017-11-21 Atyr Pharma, Inc. PEGylated aspartyl-tRNA synthetase polypeptides
US9688978B2 (en) 2011-12-29 2017-06-27 Atyr Pharma, Inc. Aspartyl-tRNA synthetase-Fc conjugates
US9587235B2 (en) 2013-03-15 2017-03-07 Atyr Pharma, Inc. Histidyl-tRNA synthetase-Fc conjugates
US10472618B2 (en) 2013-03-15 2019-11-12 Atyr Pharma, Inc. Histidyl-tRNA synthetase-Fc conjugates
US10711260B2 (en) 2013-03-15 2020-07-14 Atyr Pharma, Inc. Histidyl-tRNA synthetase-Fc conjugates
US10093915B2 (en) 2013-03-15 2018-10-09 Atyr Pharma Inc. Histidyl-tRNA synthetase-Fc conjugates
US11072787B2 (en) 2013-03-15 2021-07-27 Atyr Pharma Inc. Histidyl-tRNA synthetase-Fc conjugates
US11767520B2 (en) 2017-04-20 2023-09-26 Atyr Pharma, Inc. Compositions and methods for treating lung inflammation

Similar Documents

Publication Publication Date Title
WO2001019999A1 (fr) Gene codant une nouvelle threonyl-arnt synthase, ses utilisations et procedes de preparation
JPH1156376A (ja) ヒトＩκＢ−β
WO2001038371A1 (fr) Nouveau polypeptide glutamate arnt synthetase 58 d'origine humaine et polycnucleotide codant pour ce polypeptide
US6908765B1 (en) Polypeptide—human SR splicing factor 52 and a polynucleotide encoding the same
US6919427B1 (en) Polypeptide-rna binding protein 33 and polynucleotide encoding said polypeptide
JP2001517940A (ja) セリン／スレオニンプロテインキナーゼ
WO2001029228A1 (fr) Nouveau polypeptide, caseine kinase humaine 48, et polynucleotide codant pour ce polypeptide
US6994996B1 (en) Polypeptide, human vacuolar H+ -ATPase C subunit 42 and polynucleotide encoding it
WO2001019864A1 (fr) Polynucleotides codant pour des nouvelles proteines humaines du recepteur de l'angiotensine ii-1, leur procede de preparation et leur utilisation
WO2001038545A1 (fr) Nouveau polypeptide, acetyle galactosyle transferase 45 humain et polynucleotide codant ce polypeptide
US20040005658A1 (en) Novel polypeptide-human an1-like protein 16 and the polynucleotide encoding the same
WO2001031024A1 (fr) Nouveau polypeptide, threonine synthetase 71, et polynucleotide codant pour ce polypeptide
CN1375007A (zh) 编码一种新的苏氨酰转移核糖核酸合成酶的基因及其应用和制备方法
WO2001032699A1 (fr) Nouveau polypeptide, nouvelle udp glucose-glycoproteine glucosyltransferase (« biohugtr »), et polynucleotide codant pour ce polypeptide
WO2001038369A1 (fr) Nouveau polypeptide porteur tricarboxylate 39 du rat- et polynucleotide codant ledit polypeptide
WO2001030840A1 (fr) Nouveau polypeptide, une proteine 57 a doigt de zinc, et polynucleotide codant pour ce polypeptide
WO2001023423A1 (fr) Nouveau gene comprenant le domaine ww et codant le polypeptide humain interagissant avec l'huntingtine, methode de production dudit gene et application correspondante
WO2001027283A1 (fr) Nouveau polypeptide, proteine 16 de type transcriptase humaine inverse, et polynucleotide codant pour ce polypeptide
WO2001038389A1 (fr) Nouvelle proteine ribosomique l14.22 a base d'un polypeptide et polynucleotide codant cette proteine
WO2001027285A1 (fr) Nouveau polypeptide, methyltransferase humaine dpb 41 et polynucleotide codant pour ce polypeptide
WO2001030837A1 (fr) Nouveau polypeptide, galectine 15, et polynucleotide codant pour ce polypeptide
WO2001038370A1 (fr) Nouvelle sous-unite 49 de l'activateur de transcription polypeptidique et polynucleotide codant ce polypeptide
WO2001032862A1 (fr) Nouveau polypeptide, proteine humaine 20 ribosome s4, et polynucleotide codant pour ce polypeptide
WO2001027148A1 (fr) Nouveau polypeptide, facteur homo 56 riche en glutamine(q), et polynucleotide codant pour ce polypeptide
WO2001038380A1 (fr) Nouveau polypeptide, proteine humaine 56 de regulation du noyau cellulaire, et polynucleotide codant pour ce polypeptide

Legal Events

Date Code Title Description
AK Designated states

Kind code of ref document: A1

Designated state(s): CN JP US

AL Designated countries for regional patents

Kind code of ref document: A1

Designated state(s): AT BE CH CY DE DK ES FI FR GB GR IE IT LU MC NL PT SE

DFPE Request for preliminary examination filed prior to expiration of 19th month from priority date (pct application filed before 20040101)
121 Ep: the epo has been informed by wipo that ep was designated in this application
WWE Wipo information: entry into national phase

Ref document number: 008128731

Country of ref document: CN

122 Ep: pct application non-entry in european phase
NENP Non-entry into the national phase

Ref country code: JP

点击 这是indexloc提供的php浏览器服务，不要输入任何密码和下载