Biochemical characterization of a thrombin-like enzyme and a fibrinolytic serine protease from snake (Agkistrodon saxatilis) venom.
A thrombin-like enzyme and a fibrinolytic serine protease were purified to homogeneity from the venom of a Korean snake Agkistrodon saxatilis emelianov. Both the purified enzymes migrated as a single protein band corresponding to 39 kDa in SDS-PAGE. However, the molecular mass was reduced to 28 kDa by enzymatic removal of the N-linked carbohydrates in those two different enzyme species. Although the thrombin-like enzyme and the fibrinolytic protease show homologous features in their molecular sizes and N-terminal amino acid sequences, yet they can be clearly distinguished from each other in terms of substrate specificity, susceptibility to inhibitors and fibrinogen degradation. It is postulated that these two enzymes are capable of functioning in a cooperative manner to effectively remove fibrinogen and consequently to reduce the blood viscosity.
Koh
Y S
YS
Department of Biochemistry, College of Science and Bioproducts Research Center, Yonsei University, Seoul, South Korea.
Chung
K H
KH
Kim
D S
DS
D000595:Amino Acid Sequence; D003435:Crotalid Venoms / Q000737:chemistry*; D005343:Fibrinolytic Agents / Q000737:chemistry / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D012697:Serine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification*; D013379:Substrate Specificity; D013917:Thrombin / Q000737:chemistry / Q000302:isolation & purification*
D003435:Crotalid Venoms; D005343:Fibrinolytic Agents; D012697:Serine Endopeptidases; D013917:Thrombin