Isoforms of a highly specific B beta-chain fibrinogenase from the venom of Crotalus atrox: preliminary observations.
Three variants of a Crotalus atrox venom enzyme that cleaves primarily the Arg42 - Ala bond of the B beta-chain of human fibrinogen were separated by high-performance liquid chromatography and were shown by N-terminal sequence analysis to be amino acid isoforms. All are single-chain glycoproteins whose approximate molecular weights lie between 26,000 and 28,000. The isoenzymes also cleaved the A alpha-chain at Arg491 - His, though much more weakly, with strengths for both bonds that varied among the isoforms.
Pirkle
H
H
Department of Pathology, Medical Sciences I, University of California, Irvine 92717.
Henschen
A
A
Theodor
I
I
Cunnan
J
J
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D007527:Isoenzymes / Q000235:genetics / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D012697:Serine Endopeptidases / Q000235:genetics; D012911:Snakes / Q000235:genetics / Q000378:metabolism*; D013917:Thrombin / Q000145:classification / Q000235:genetics / Q000302:isolation & purification*
D007527:Isoenzymes; D012697:Serine Endopeptidases; C062780:catroxobin; D013917:Thrombin