Open AccessMonoclonal antibodies inhibitory to human plasmin
Author(s) -
SIM PhengSiew,
FAYLE David R. H.,
DOE William F.,
STEPHENS Ross W.
Publication year - 1986
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1986.tb09787.x
Subject(s) - plasmin , monoclonal antibody , urokinase , plasminogen activator , chemistry , fibrinolysis , antibody , microbiology and biotechnology , biochemistry , fibrinolysin , affinity chromatography , enzyme , biology , immunology , endocrinology , medicine , genetics
Four monoclonal antibodies raised against purified human plasminogen were characterized for their effects on the activation of plasminogen and on three enzymic properties of plasmin: (a) thioesterolysis, (b) fibrinolysis, (c) conversion of high‐ M r urokinase to its low‐ M r form. None of the monoclonal antibodies inhibited plasminogen (plg) activation by urokinase. The monoclonal antibodies characterized in this study fell into three groups. Anti‐plg 1 inhibited (a), (b) and (c), while anti‐plg 2 inhibited activities (a), (b) and (c) to varying degrees but also formed complexes with plasmin that were stable to sodium dodecyl sulphate. Anti‐plg 3 and anti‐plg 4 inhibited only activity (c). Selective use of these monoclonal antibodies demonstrated unequivocally that plasmin mediates the activation of the proenzyme form of urokinase‐type plasminogen activator. Besides their use in affinity chromatography, therefore, these antibodies are valuable for defining the role of plasmin in the mechanisms of extracellular matrix degradation.