Author/Editor     Aragon-Ortiz, F; Gubenšek, F
Title     A thrombin-like enzyme from bushmaster (Lachesis muta stenophyrs) venom
Type     članek
Source     Toxicon
Vol. and No.     Letnik 31, št. 11
Publication year     1993
Volume     str. 1435-43
Language     eng
Abstract     The clotting enzyme (Stenoxobin), from the venom of Lachesis muta stenophyrs, was purified by gel chromatography on Bio-gel P-100 followed by agmatine CH-Sepharose-4B and FPLC on Mono Q column. By SDS polyacrylamide gel electrophoresis the mol. wt was found to be 37,000. The enzyme is a glycoprotein with 1.6 moles of sialic acid per mole of protein and has an average content of 7.0 percent of neutral carbohydrates. The clotting and esterolytic (BAEE) activities were 843 NIH units/mg and 60.1 +/- 1.2 OD225 ml/min/mg, respectively, and could not be inhibited by heparin or hirudin. Amino acid analysis revealed a low content of tryptophan and a high content of acid residues. Stenoxobin acts upon human fibrinogen by releasing consecutively fibrinopeptides A and B from the alpha- and beta-chains of fibrinogen.
Descriptors     COAGULANTS
CROTALID VENOMS
GLYCOPROTEINS
COAGULANTS
ELECTROPHORESIS, POLYACRYLAMIDE GEL
GLYCOPROTEINS
THROMBIN