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Detection of glycoprotein IIb and IIIa by monoclonal antibodies
Author(s) -
Thurlow P. J.,
Barlow B.,
Connellan J. M.,
McKenzie I. F. C.
Publication year - 1983
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1983.tb01230.x
Subject(s) - platelet , monoclonal antibody , glycoprotein , antibody , radioimmunoassay , microbiology and biotechnology , platelet membrane glycoprotein , chemistry , bone marrow , platelet activation , biochemistry , immunology , biology
S ummary . Murine monoclonal antibodies were produced against human platelet membranes and screened on platelets by a 125 I protein A radioimmunoassay. Several clones produced platelet specific antibodies as they showed no reaction with peripheral blood lymphocytes, neutrophils, bone marrow (excluding megakaryocytes) or several cell lines. Two antibodies (designated anti‐HuPl‐mla and anti‐HuPl‐mlb) were of particular interest in that although platelet specific they were non‐reactive with platelets from a thrombasthenic patient. In functional assays these two antibodies could specifically inhibit ADP and collagen induced aggregation of platelets and release of ATP, retard platelet aggregation and ATP release induced by epinephrine, and inhibit ADP induced platelet fibrinogen binding. These two antibodies appear to recognize glycoproteins IIb and IIIa as analysis by SDS‐PAGE using radiolabelled membranes revealed a two chain structure of molecular weight 112 000 and 122 000 daltons when run after reduction and 87 000 and 140 000 daltons non‐reduced.