-transparent.png){kind=logo}
A method is described by which the heavy chain of human plasmin, obtained by partial reduction of urokinase-activated plasminogen with 2-mercaptoethanol, is adsorbed on lysine coupled to polyacrylamide. The heavy chain is recovered from the adsorbent by elution with 6-aminohexanoic acid (yield 60-65%). Sulfhydryl titrations of the heavy chain showed that the partial reduction involved primarily the cleavage of the sole interchain disulfide bridge of plasmin. Dodecylsulfate-polyacrylamide electrophoresis gave essentially a single band corresponding to a component of about 60000 molecular weight. The NH2-terminal amino acid was predominantly threonine. 6-Aminohexanoic acid at different concentrations caused significant variations of the sedimentation and diffusion constants of the heavy chain indicating inhibitor-induced conformational alterations of the protein. The present results suggest that in plasmin only the heavy chain is capable of interacting with 6-aminohexanoic acid, and it appears that it is primarily this chain which plays an important role in the inhibition of the enzyme by 6-aminohexanoic acid.
E E Rickli, and
W I Otavsky
April 1971,
The Journal of biological chemistry,
E E Rickli, and
W I Otavsky
April 1977,
The Journal of biological chemistry,
E E Rickli, and
W I Otavsky
October 1976,
European journal of biochemistry,
E E Rickli, and
W I Otavsky
April 1964,
Thrombosis et diathesis haemorrhagica,
E E Rickli, and
W I Otavsky
August 1987,
Thrombosis and haemostasis,
E E Rickli, and
W I Otavsky
March 1980,
Biochimica et biophysica acta,
E E Rickli, and
W I Otavsky
May 1978,
Biochemistry,
E E Rickli, and
W I Otavsky
December 1986,
Thrombosis and haemostasis,
E E Rickli, and
W I Otavsky
June 1983,
Proceedings of the National Academy of Sciences of the United States of America,
E E Rickli, and
W I Otavsky
January 1982,
Molecular immunology,
