Preparation and characterization of proteolyzed forms of human alpha-thrombin.
The kinetics of the tryptic digestion of human alpha-thrombin were studied. Based on the results of these studies a procedure for the preparation of highly purified, active human beta-thrombin was developed. This beta-thrombin contained less than 5% of other thrombin forms, was active towards tripeptidyl paranitroanilide substrates, but had lost more than 99% of its fibrinogen cleaving activity. Protein-chemical characterization of beta-thrombin showed that it had been cleaved at a single site (Arg73-Asn74) in the beta-chain, in contrast to human beta-thrombin obtained by autolysis, which is cleaved at both Arg-62 and Arg-73.
Braun
P J
PJ
Friedrich Miescher Institut, Basel, Switzerland.
Hofsteenge
J
J
Chang
J Y
JY
Stone
S R
SR
D000596:Amino Acids / Q000032:analysis; D006801:Humans; D007700:Kinetics; D013917:Thrombin / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism
D000596:Amino Acids; D014357:Trypsin; D013917:Thrombin