A novel alpha-type fibrinogenase from Agkistrodon rhodostoma snake venom.
By means of CM-Sephadex C-50 column chromatography, gel-filtration on sephadex G-75 and Sephacryl S-200 columns, a purified fibrinogenase, kistomin, was obtained from venom of Agkistrodon rhodostoma. It was a single peptide-chain with a molecular mass of about 21,800 Da containing about 202 amino-acid residues as revealed by amino acid analysis. Kistomin preferentially cleaved A alpha- and subsequently the gamma-chain of fibrinogen, leaving the B beta-chain unaffected. Its fibrinogenolytic activity was estimated to be 36.6 +/- 4.5 mg/min per mg protein and was inhibited by the pretreatment of EDTA, suggesting that it is a metalloproteinase. Its fibrinogenolytic activity in platelet-poor plasma is much less potent as compared to that in purified fibrinogen solution. It inhibited ristocetin-induced aggregation of human platelets in a dose-dependent manner in the presence of von Willebrand factor.
Huang
T F
TF
Pharmacological Institute, College of Medicine, National Taiwan University, Taipei.
Chang
M C
MC
Peng
H C
HC
Teng
C M
CM
D000596:Amino Acids / Q000032:analysis; D000721:Ancrod / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D005591:Chemical Fractionation; D003435:Crotalid Venoms / Q000737:chemistry*; D005340:Fibrinogen / Q000737:chemistry; D010975:Platelet Aggregation Inhibitors / Q000494:pharmacology; D012310:Ristocetin / Q000037:antagonists & inhibitors
D000596:Amino Acids; D003435:Crotalid Venoms; D010975:Platelet Aggregation Inhibitors; D012310:Ristocetin; D005340:Fibrinogen; D000721:Ancrod