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WO1991008485A1 - Immunoanalyse pour la detection des anticorps aux agents de maladies infectieuses - Google Patents

Immunoanalyse pour la detection des anticorps aux agents de maladies infectieuses Download PDF

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Publication number
WO1991008485A1
WO1991008485A1 PCT/US1990/006680 US9006680W WO9108485A1 WO 1991008485 A1 WO1991008485 A1 WO 1991008485A1 US 9006680 W US9006680 W US 9006680W WO 9108485 A1 WO9108485 A1 WO 9108485A1
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WO
WIPO (PCT)
Prior art keywords
porous member
antibodies
fluid
binding
test sample
Prior art date
Application number
PCT/US1990/006680
Other languages
English (en)
Inventor
Gordon R. Whiteley
T. Philip Wong
Original Assignee
Pb Diagnostic Systems, Inc.
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 Pb Diagnostic Systems, Inc. filed Critical Pb Diagnostic Systems, Inc.
Priority to AU67598/90A priority Critical patent/AU647428B2/en
Priority to JP3500578A priority patent/JPH05503772A/ja
Publication of WO1991008485A1 publication Critical patent/WO1991008485A1/fr

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Classifications

    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
    • G01N33/569—Immunoassay; Biospecific binding assay; Materials therefor for microorganisms, e.g. protozoa, bacteria, viruses
    • G01N33/56983—Viruses
    • G01N33/56988—HIV or HTLV
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
    • G01N33/543—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals
    • G01N33/54366—Apparatus specially adapted for solid-phase testing

Definitions

  • the invention relates to a method for assaying for antibodies to infectious diseases and, more particularly, to a method which utilizes a porous solid phase.
  • Various methods for the detection of antibodies to infectious diseases e.g., antibodies to the HIV I and II (AIDS) viruses, are known for confirmation of acute disease, exposure to a disease or immunity to a disease.
  • the known methods for the detection of antibodies to the AIDS virus include enzyme-linked immunosorbant assays (ELISA), Western Blot and immunofluorescent techniques.
  • ELISA enzyme-linked immunosorbant assays
  • An established method for blood donor screening is to first carry out an ELISA followed by confirmation of positive results by the Western Blot technique.
  • a typical ELISA technique involves reacting a test sample with an antigen reagent generally obtained from disrupted whole or density banded HIV I and II.
  • an antigen reagent generally obtained from disrupted whole or density banded HIV I and II.
  • the antigen reagent is coated onto wells of a microtiter plate. After washing to remove unbound antibodies, anti-human IgG antiserum conjugated with an enzyme is added to the wells and incubated. After an appropriate incubation period, an enzyme substrate is added to the mixture and a detectable, measurable product is formed in the presence of antibodies to HIV I and II.
  • an assay technique for the detection of antibodies to infectious diseases which utilizes as the solid phase a porous member to which there is immobilized a binding material capable of binding to the antibodies of a desired subclass or subclasses, including the antibodies to the infectious disease of interest, which are present in the fluid sample.
  • the assay method when the test sample includes antibodies to the infectious disease of interest, there is formed a ternary complex of the immobilized binding material, the antibody of interest and a labeled detector material, e.g., a labeled antigen, which is specific to the antibody of interest.
  • a labeled detector material e.g., a labeled antigen
  • the assay method of the invention may be used for any serology test, that is, any test for antibodies to an infectious disease.
  • Typical infectious diseases for which screening may be carried out according to this assay technique include rubella, cytomegalovirus, toxoplasma, lyme disease, herpes I and II, Epstein-Barr virus, HTLV, HIV, chlamydia and hepatitis.
  • the assay method of the invention is rapid, sensitive and specific and, in a preferred embodiment, can be carried out in a single test module format which allows for total test containment.
  • Fig. 1 is a simplified isometric view of a single test module which can be utilized for the assay method.
  • a porous member is utilized as the solid phase for the assay method and to this member there is immobilized a binding material which is capable of binding to the antibodies of a desired subclass or subclasses, including the antibodies of interest, which are present in the test sample.
  • a binding material which is capable of binding to the antibodies of a desired subclass or subclasses, including the antibodies of interest, which are present in the test sample.
  • the porous member may be a porous membrane, a fibrous mesh pad or the like and may be of any suitable material such as glass, polymeric materials, paper, etc.
  • the binding material which is immobilized by the porous member may be any suitable material which is capable of binding antibodies of a desired subclass or subclasses in the test sample.
  • suitable binding materials include proteins such as protein A and protein G, both naturally occurring and genetically engineered, polyclonal antibodies such as goat anti- human IgG and monoclonal antibodies such as mouse anti- human IgG.
  • binding material may be used also.
  • the amount of binding material necessary for any particular assay varies with the assay and can be optimized by conventional experimental scoping techniques. It is preferred to calculate the amount of binding material necessary to bind all, or substantially all, of the antibodies of a desired subclass or subclasses in the patient sample and apply an excess of that amount to the porous member.
  • the binding material may be applied to the porous member and immobilized thereto by any of various known techniques including physical entrapment and chemical bonding.
  • a solution of the binding material can be applied to the porous member and the member subsequently dried to provide a porous member having the binding material distributed throughout and held therein by the structure of the member.
  • the binding material can be chemically bound to or adsorbed on polymeric particles and the fibrous mesh pad impregnated with the paniculate matter. In this manner the binding material is immobilized to the porous member and remains there throughout the assay method.
  • a preferred technique is to apply a solution of the binding material to the porous member and subsequently heat the member to fix the binding material thereto.
  • the assay method of the invention also involves the use of a labeled detector material which will bind specifically to the antibody of interest and not substantially to any of the other antibodies present in the test sample.
  • the detector material of the labeled conjugate may be of any type which is capable of binding specifically to the antibody of interest including recombinant or purified cultured antigens, analogues thereof or synthetically prepared peptide sequences. Synthetically prepared peptide sequences are preferred because of their binding specificity. For HIV assays it is preferred to utilize labeled HIV I and II peptide sequences because of their lack of cross-reactive material and safety in handling.
  • any of the labels known for use in immunometric assays may be utilized including, for example, fluorescent moieties, enzymes, chemiluminescent moieties and radioactive materials. Any change in fluorescence, chemiluminescence, radioactivity or other change in visible or near visible radiation can be exploited. Thus, the label may be directly or indirectly detectable. Where the label is an enzyme it can be one which interacts with a substrate to cause a change in absorption where the substrate is a chromogen, in fluorescence if the substrate is a fluorophore, in chemiluminescence where the substrate is a chemiluminescent precursor or in phosphorescence where the substrate is a phosphor.
  • test sample may be applied initially to the porous member followed by an incubation step to allow the desired subclass or subclasses of antibodies in the sample fluid to interact and bind to the binding material on the porous member.
  • a solution of the conjugate is then applied to the porous member followed by an incubation step.
  • a volume of fluid sample e.g. about 10 ul, is added to a solution of the labeled conjugate in a buffer, and the mixture incubated to allow the interactions between the labeled conjugate and antibody of interest to take place.
  • An aliquot of this reaction mixture is then deposited on the porous member followed by another incubation step to allow the interactions between the binding material and the antibodies in the fluid sample to occur. This embodiment is preferred because of the rapid liquid phase kinetics of the first reaction.
  • any free labeled conjugate is removed from the reaction zone such as by a wash step wherein a wash solution is applied to the porous member.
  • the wash solution may be applied to the porous member in any way including depositing the wash solution on the center of the porous member or by applying it to an outer periphery of the member.
  • any bound labeled conjugate is detected by appropriate means.
  • the label maybe directly or indirectly detectable.
  • the substrate solution which is applied to the porous member to render the label detectable may also be utilized as the wash solution to remove from the porous member any free labeled conjugate.
  • the method is practiced with a single test capillary assay module which is suitable for use in automated analytical test instruments. Referring now to Fig. 1 there is illustrated a self-contained assay module, or element, 10 which carries all of the test reagents, except for the sample fluid, necessary for a particular assay.
  • This preferred assay element includes a plurality of chambers in a housing 22 wherein a first chamber serves as a front reservoir 24 for the storage of the labeled conjugate solution.
  • the solution is covered with a frangible or puncturable foil layer (not shown).
  • a second of the chambers serves as a back reservoir 26 for the storage of a substrate solution which is also covered with a similar foil layer (not shown).
  • An optional third chamber serves as a mixing bowl 28 for the mixing of reagents and a fourth chamber forms part of a dispenser 30 which is utilized to dispense the substrate solution to one end of the porous member 32.
  • a chamber 34 within the housing 22 wherein there is arranged an absorbing material for absorbing fluid removed from the porous member such as by a wash fluid as it propagates through the porous member 32.
  • the porous member 32 is a thin porous member possessing an intercommunicating network of openings throughout such that a fluid deposited on the member will propagate throughout the member because of capillary action.
  • the thin porous member 32 may be any suitable element such as a porous membrane, a fibrous mesh pad or the like and may be of any suitable material such as glass, polymeric materials, paper, etc.
  • porous member 32 comprises a nonwoven glass fiber mesh having very thin fibers such as on the order of about 1 micrometer.
  • the porous member 32 is mounted within a guide (not shown) formed within the housing 22 and having top and bottom surfaces which are spaced apart a distance sufficient to support the member 32.
  • a guide (not shown) formed within the housing 22 and having top and bottom surfaces which are spaced apart a distance sufficient to support the member 32.
  • the spacing between the top and bottom surfaces of the guide may be in the range of from about 0.30 mm to about 0.60 mm; the preferred spacing is about 0.40 mm.
  • the porous member 32 extends from the dispenser 30 to the chamber 34 which holds the absorbing material.
  • the dispenser chamber 30 is configured as a well for holding a fluid, the dispenser 30 including a port at the bottom of the well and means for allowing communication of fluid from the bottom of the well into the porous member 32.
  • Liquid absorbing material 36 which may be any suitable material, is located within chamber 34 and forms a part of the chamber 34 for taking up fluid expelled from the porous member 32 and the guide area, or reaction zone.
  • Absorbing material 36 is located contiguous porous member 32 and in a preferred embodiment (as illustrated) is formed conveniently as an extension of the porous material folded back and forth on itself.
  • the housing 22 also preferably includes a chamber 38 which is positioned immediately above the top horizontal surface of porous member 32 and has a port at the bottom periphery thereof to allow fluid to be delivered to the porous member 32.
  • the housing 22 may include a transparent window area (not shown) positioned immediately below the bottom horizontal surface of porous member 32 to provide access for the illumination used to measure any detectable change effected in the porous member as a result of the assay method or preferably an opening in the housing to permit readout illumination to be directed onto the porous member without having to pass through the material of which the housing is comprised.
  • the sample fluid tested according to the assay method of the invention may be any including whole blood, plasma or serum.
  • a small amount e.g., about 10 ul of serum taken from a patient sample is added to an enzyme-labeled conjugate solution, e.g., about 190 ul, in chamber 24 via a pipette which perforates the foil layer over chamber 24 and the assay element is allowed to incubate for the necessary period of time.
  • an enzyme-labeled conjugate solution e.g., about 190 ul
  • the amount of patient sample required can vary from assay to assay.
  • an aliquot e.g.
  • the reaction mixture in chamber 24 is aspirated into a clean pipette tip and then deposited on the upper surface of porous member 32 through chamber 38,.
  • the sample fluid is drawn throughout porous member 32 by capillary action and the assay module is again allowed to incubate for a suitable period to allow the interactions to take place.
  • the foil layer covering chamber 26 to form a seal over the substrate solution in the chamber is perforated by a pipette carrying a clean tip and a desired volume of the substrate solution, typically about 75 ul, is aspirated into the pipette tip.
  • the substrate solution is then deposited into chamber 30 from where it is allowed to come into contact with one end of porous member 32 and then drawn throughout the member by capillary action.
  • the assay module is then allowed to incubate to permit the reaction between the substrate material and any bound enzyme label to take place. It is apparent that the substrate solution is also utilized as a wash fluid in this embodiment. As the substrate solution propagates through porous member 32 it forces any free enzyme-labeled conjugate together with the fluid out of the porous member and into absorber chamber 34 where they are taken up by absorber material 36.
  • the signal provided by the species liberated by the reaction between the substrate material and the enzyme for example, a fluorescent species, is then read by means of a suitable readout means, e.g., a fluorometer. Both qualitative and quantitative results can be obtained with this method.
  • the method of the invention as carried out with the preferred assay module illustrated can be practiced with an automated assay instrument thus providing a totally self- contained test which requires a minimum of operator involvement and which eliminates operator variability.
  • a preferred assay module of the type illustrated in Fig. 1 is disclosed and claimed in copending, commonly assigned application Serial No. 354,026 filed May 19, 1989, the entire disclosure of which is incorporated by reference herein.
  • EXAMPLE I Assays for HIV antibodies in patient samples of serum or plasma were carried out according to the method of the invention in accordance with the following procedure.
  • the fibrous mesh has a thickness of approximately 0.42 mm.
  • the amount of binding material applied to the mesh was about seven times the amount theoretically calculated to be necessary to bind all of the IgG antibodies in a typical patient sample.
  • the assay module was dried at 75°C for ten minutes to fix the binding material to the fibrous pad.
  • a total of 10 ul of sample was added to 190 ul of HIV specific peptide which was previously covalently conjugated to alkaline phosphatase and diluted to the desired concentration in a buffer consisting of 50 mM tris [hydroxymethyl] - aminomethane, (TRIS) pH 7.6, 150 mM NaCI, 1 mM MgCI 2 , 0.1 mM ZnCI 2 , 0.1 % Triton X 100, 1 % gelatin and 1 % BSA. The reaction mixture was incubated for six minutes at 37°C.
  • TMS tris [hydroxymethyl] - aminomethane
  • Readings were taken of the reaction zone at regular intervals over a three minute period using a front surface f luorometer by directing 360 nm radiation through an opening in the assay module beneath the reaction zone and collecting the reflected 450 nm radiation.
  • the increase in fluorescence a function of the amount of enzyme-labeled conjugate bound by the peptide-specific antibody in the sample, was calculated.
  • the result obtained was compared to the results obtained with defined negative and positive calibrators and was determined to be positive or negative on the basis of a determined cutoff value.
  • a total of 132 patient samples were determined to be positive for HIV antibodies by conventional ELISA and
  • EXAMPLE HI Specimens constituting panel "c" were obtained from Boston Biomedica, Inc. These specimens were serially obtained from one patient and are identified from day 1 in Table III. The specimens were tested according to the method described in Example I. The results obtained, which are shown in Table 111, show that the test method of the invention can detect a positive sample consistently on day 107 which is substantially earlier (from 28 to 35 days) than most conventional tests according to published data. TABLE
  • the present invention provides a solid phase immunoassay for HIV antibodies which has the sensitivity and specificity of conventional ELISA methods.
  • the present assay method provides a more rapid analysis which is not as susceptible to specimen matrix or wash techniques and volumes as are conventional assay methods. Less specimen handling is required by this assay method than is the case in conventional ELISA methods thus resulting in less potential exposure to infectious material.

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  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Immunology (AREA)
  • Engineering & Computer Science (AREA)
  • Molecular Biology (AREA)
  • Biomedical Technology (AREA)
  • Chemical & Material Sciences (AREA)
  • Hematology (AREA)
  • Urology & Nephrology (AREA)
  • Food Science & Technology (AREA)
  • General Physics & Mathematics (AREA)
  • Cell Biology (AREA)
  • Biotechnology (AREA)
  • Medicinal Chemistry (AREA)
  • Physics & Mathematics (AREA)
  • Analytical Chemistry (AREA)
  • Biochemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • Microbiology (AREA)
  • Pathology (AREA)
  • Virology (AREA)
  • AIDS & HIV (AREA)
  • Tropical Medicine & Parasitology (AREA)
  • Investigating Or Analysing Biological Materials (AREA)
  • Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
  • Peptides Or Proteins (AREA)

Abstract

On décrit une analyse rapide, sensible et spécifique permettant de détecter des anticorps aux maladies infectieuses. La méthode fait appel à un élément poreux sur lequel est immobilisé une matière de liaison pouvant se lier aux anticorps d'une sous-classe ou des sous-classes données, présentes dans l'échantillon d'essai. Selon la méthode décrite, lorsque l'échantillon renferme des anticorps à la maladie infectieuse d'intérêt il se forme un complexe ternaire de la matière de liaison, de l'anticorps d'intérêt et d'une matière de détection étiquetée, par exemple un antigène étiqueté, qui est spécifique à l'anticorps d'intérêt. Après enlèvement de la matière de détection étiquetée de la zone de réaction, on détecte toute matière de détection étiquetée afin d'obtenir une indication de la présence des anticorps d'intérêt.
PCT/US1990/006680 1989-12-01 1990-11-15 Immunoanalyse pour la detection des anticorps aux agents de maladies infectieuses WO1991008485A1 (fr)

Priority Applications (2)

Application Number Priority Date Filing Date Title
AU67598/90A AU647428B2 (en) 1989-12-01 1990-11-15 Immunoassay for antibodies to infectious disease agents
JP3500578A JPH05503772A (ja) 1990-11-15 1990-11-15 固相血清学的検定方法

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
US44502589A 1989-12-01 1989-12-01
US445,025 1989-12-01

Publications (1)

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WO1991008485A1 true WO1991008485A1 (fr) 1991-06-13

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EP (1) EP0456794A1 (fr)
AU (1) AU647428B2 (fr)
CA (1) CA2030232A1 (fr)
WO (1) WO1991008485A1 (fr)

Cited By (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1994024560A1 (fr) * 1993-04-14 1994-10-27 International Murex Technologies Corporation Dosage immunologique
EP0636886A2 (fr) * 1993-06-29 1995-02-01 Behring Diagnostics Inc. Composition d'étalonnage ou de contrôle pour un essai sérologique d'IgM
GB2282884A (en) * 1993-04-14 1995-04-19 Int Murex Tech Corp Immunoassay
EP2176662A2 (fr) * 2007-07-30 2010-04-21 The Arizona Board Of Regents, A Body Corporate Of The State Of Arizona Acting For And Behalf Of Procedes et dispositifs pour la detection de biofilm
US8697375B2 (en) 2008-09-02 2014-04-15 University Of Maryland, Baltimore In vivo biofilm infection diagnosis and treatment

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EP0008473A1 (fr) * 1978-08-24 1980-03-05 Akzo N.V. Procédé pour la détection et/ou la détermination d'une immunoglobuline spécifique d'un antigène, réactifs immunologiques et trousse de réactifs à utiliser dans ce procédé de détermination
US4273756A (en) * 1978-07-28 1981-06-16 Abbott Laboratories Immunoassay for class specific antibodies
US4292403A (en) * 1978-08-24 1981-09-29 Akzona Incorporated Detection and/or determination of IgM, IgA, IgD and IgE immunoglobulins
EP0044041A1 (fr) * 1980-07-14 1982-01-20 Hoechst Aktiengesellschaft Méthode pour la liaison et la séparation dans les radioimmunoessais compétitifs et réactif pour cette méthode
WO1987006345A1 (fr) * 1986-04-11 1987-10-22 Murex Corporation Immuno-annalyse de mesure colorimetrique de proportionnalite
EP0280211A2 (fr) * 1987-02-23 1988-08-31 Roche Diagnostics GmbH Procédé pour déterminer des anticorps
EP0286371A2 (fr) * 1987-04-07 1988-10-12 Syntex (U.S.A.) Inc. Dispositif pour les essais immunologiques
DE3717401A1 (de) * 1987-05-23 1988-12-08 Behringwerke Ag Einschritt-immuntest zur bestimmung von antigen-spezifischen antikoerpern aus einer der immunglobulin-klassen a, m, d oder e und dazu geeignetes mittel
EP0306336A2 (fr) * 1987-09-04 1989-03-08 Syntex (U.S.A.) Inc. Dispositif d'essai à multiples orifices
EP0306772A1 (fr) * 1987-09-11 1989-03-15 Abbott Laboratories Dispositif pour essai de fixation chromatographique à écoulement latéral
EP0346119A2 (fr) * 1988-06-08 1989-12-13 Cambridge Bioscience Corporation Essai anti-FC pour détecter des anticorps

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AU610095B2 (en) * 1986-11-19 1991-05-16 Genetic Systems Corporation Membrane affinity concentration immunoassay
CA2056447A1 (fr) * 1990-03-28 1991-09-29 Stefan Gavojdea Methode de prelevement d'anticorps et de detection d'une espece d'anticorps particuliere dans un echantillon de liquide, et dispositif permettant d'appliquer ladite methode, accompagne d'une trousse dans laquelle se trouve ce dispositif

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EP0008473A1 (fr) * 1978-08-24 1980-03-05 Akzo N.V. Procédé pour la détection et/ou la détermination d'une immunoglobuline spécifique d'un antigène, réactifs immunologiques et trousse de réactifs à utiliser dans ce procédé de détermination
US4292403A (en) * 1978-08-24 1981-09-29 Akzona Incorporated Detection and/or determination of IgM, IgA, IgD and IgE immunoglobulins
EP0044041A1 (fr) * 1980-07-14 1982-01-20 Hoechst Aktiengesellschaft Méthode pour la liaison et la séparation dans les radioimmunoessais compétitifs et réactif pour cette méthode
WO1987006345A1 (fr) * 1986-04-11 1987-10-22 Murex Corporation Immuno-annalyse de mesure colorimetrique de proportionnalite
EP0280211A2 (fr) * 1987-02-23 1988-08-31 Roche Diagnostics GmbH Procédé pour déterminer des anticorps
EP0286371A2 (fr) * 1987-04-07 1988-10-12 Syntex (U.S.A.) Inc. Dispositif pour les essais immunologiques
DE3717401A1 (de) * 1987-05-23 1988-12-08 Behringwerke Ag Einschritt-immuntest zur bestimmung von antigen-spezifischen antikoerpern aus einer der immunglobulin-klassen a, m, d oder e und dazu geeignetes mittel
EP0306336A2 (fr) * 1987-09-04 1989-03-08 Syntex (U.S.A.) Inc. Dispositif d'essai à multiples orifices
EP0306772A1 (fr) * 1987-09-11 1989-03-15 Abbott Laboratories Dispositif pour essai de fixation chromatographique à écoulement latéral
EP0346119A2 (fr) * 1988-06-08 1989-12-13 Cambridge Bioscience Corporation Essai anti-FC pour détecter des anticorps

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Cited By (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1994024560A1 (fr) * 1993-04-14 1994-10-27 International Murex Technologies Corporation Dosage immunologique
GB2282884A (en) * 1993-04-14 1995-04-19 Int Murex Tech Corp Immunoassay
EP0636886A2 (fr) * 1993-06-29 1995-02-01 Behring Diagnostics Inc. Composition d'étalonnage ou de contrôle pour un essai sérologique d'IgM
EP0636886A3 (fr) * 1993-06-29 1995-11-15 Pb Diagnostic Systems Inc Composition d'étalonnage ou de contrÔle pour un essai sérologique d'IgM.
EP2176662A2 (fr) * 2007-07-30 2010-04-21 The Arizona Board Of Regents, A Body Corporate Of The State Of Arizona Acting For And Behalf Of Procedes et dispositifs pour la detection de biofilm
EP2176662A4 (fr) * 2007-07-30 2010-08-18 Univ Arizona Procedes et dispositifs pour la detection de biofilm
US8697375B2 (en) 2008-09-02 2014-04-15 University Of Maryland, Baltimore In vivo biofilm infection diagnosis and treatment

Also Published As

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CA2030232A1 (fr) 1991-06-02
AU647428B2 (en) 1994-03-24
AU6759890A (en) 1991-06-26
EP0456794A1 (fr) 1991-11-21

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