Abstract
An inhibitor (I) of the plasma proteinase plasmin (P)(EC 3.4.21.7) was partially purified from washed and lysed human blood platelets by ammani sulphate fractionation and affinity chromatography. The material contain none of the known plasma proteinase inhibitors when studied by crossed ir munoelectraphoresis (CIE) and elee troimmuno assay, but inhibited a clot lysis time assay and an esterolytic assay using the synthetic substrate 2251 (O-Val-Leu-Lys-pNA), The inhibitory activity was found in the alpha region by preparative agarose gel electrophoresis (AGE). Titration of the I preparation by active-site titrated P showed a linear relationship untj zero activity indicating a strong binding of I to P. The inhibition was complete within one minute. The I changed the mobility in AGE af activator-free P or 125-I-P from the gamma region to the alpha-2 region as demoi strated by CIE against specific immunoglobulins against plasminogen or by autoradiography. An antibody against I has been raised in rabbits. The results strongly suggests the presence in platelets of a plasmin inhibitor different from the known plasma proteinase inhibitors.
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