Inhibition of cell surface receptor-bound plasmin by alpha 2-antiplasmin and alpha 2-macroglobulin

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Regulation of streptokinase-human plasmin complex by the plasma proteinase inhibitors alpha 2-antiplasmin and alpha 2-macroglobulin is species specific and temperature dependent.

Streptokinase-plasmin complex (SkPl) was prepared with human plasminogen. Regulation of SkPl and plasmin by the plasma proteinase inhibitors, alpha 2-antiplasmin (alpha 2AP) and alpha 2-macroglobulin (alpha 2M), was studied as a function of temperature in plasminogen-depleted human plasma, mouse plasma, and solutions of purified proteins. The reaction of plasmin with proteinase inhibitors in hu...

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The human alpha 2-macroglobulin receptor: identification of a 420-kD cell surface glycoprotein specific for the activated conformation of alpha 2-macroglobulin

Ligand affinity chromatography was used to purify a cell surface alpha 2-macroglobulin (alpha 2M) receptor. Detergent extracts of human placenta were applied to an affinity matrix consisting of alpha 2M, previously reacted with methylamine, coupled to Sepharose. Elution with EDTA specifically released polypeptides with apparent molecular masses of 420 and 39 kD. In some preparations, small amou...

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Production of the modified form of human plasminogen by alpha 2-macroglobulin-plasmin complexes.

It has been speculated that the modified form of plasminogen, a precursor of proteolytic enzyme plasmin in plasma, plays an important role in fibrinolysis in the blood. The present study was undertaken to examine the production by alpha 2-macroglobulin-plasmin complexes. alpha 2-Macroglobulin-plasmin complexes were purified from urokinase-activated plasma by affinity chromatography on lysine-Se...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1991

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)98900-3