Fish plasminogen activators: their identification and characterization.

K Takahashi; Y Wakamatsu; K Ozato; Y Wakayama

doi:10.1247/csf.12.11

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Fish plasminogen activators: their identification and characterization.

K Takahashi·Y Wakamatsu·K Ozato·Y Wakayama

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Abstract

Immunoblots of proteins extracted from the skin of a small viviparous fish (Xiphophorus) showed that a monoclonal antibody against human urokinase recognizes multiple molecular weight species of antigens. The immunoaffinity-purified antigens had serine-protease activity for the hydrolysis of a chromogenic substrate and could convert human plasminogen to plasmin in a manner similar to that for human urokinase in vitro. Two antigens with apparent molecular weights of 55 and 50 kilodaltons that had been purified on a fibrin-Celite column were separable on SDS-polyacrylamide gels and were characterized as major plasminogen activators on fibrin-agar indicator plates. The 125I-tryptic peptide maps of both antigens were similar to that of human urokinase; therefore, the fish activators and human urokinase are structurally and functionally related.

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Animals Antibodies, Monoclonal Cyprinodontiformes Immunosorbent Techniques Kinetics Melanophores Molecular Weight Peptide Fragments Plasminogen Plasminogen Activators Trypsin Urokinase-Type Plasminogen Activator Journal Article Research Support, Non-U.S. Gov't

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K Takahashi, Y Wakamatsu, K Ozato, Y Wakayama. 1987. Fish plasminogen activators: their identification and characterization.. https://doi.org/10.1247/csf.12.11

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