ISSN:
1432-1912
Schlagwort(e):
Snake Venom
;
Blood Coagulation
;
Prothrombin
;
Hemorrhage
;
Proteolysis
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Medizin
Notizen:
Summary 1. The procoagulant from Echis carinatus venom, which is known to convert prothrombin into thrombin, has been purified by chromatography on calcium hydroxylapatite and DEAE cellulose. Final purification, when necessary, can be achieved by disc gel electrophoresis. A final concentration of 0.5 μg/ml coagulates human citrate plasma in 70 sec. 2. The bulk of hemorrhagic, caseinolytic and fibrinogenolytic activities present in the starting venom is removed during purification, but the procoagulant causes some fibrinogenolysis, gelatinolysis, caseinolysis and hemorrhage, even when homogenous in disc gel electrophoresis. This argues for a proteolytic nature of the procoagulant activity. It is resistant against diisopropyl fluorophosphate and is not, therefore, an esteroprotease. Other protease inhibitors (from soy bean, lima bean, bovine pancreas and bovine serum) are also without effect. 3. The molecular weight is approximately 86 000, as determined by gel filtration. On isoelectric focusing in solution, its isoelectric point is pH 4.4±0.1. The procoagulant is relatively unstable; for instance, its pH-stability is restricted to values between 6 and 10.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/BF00501247
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