Isolation and characterization of an anticoagulant proteinase, cerastase F-4, from Cerastes cerastes (Egyptian sand viper) venom.
An anticoagulant protease, Cerastase F-4, was isolated from the venom of Cerastes cerastes (Egyptian sand viper) by a combination of gel filtration, ion-exchange chromatography, and HPLC. Homogeneity of the purified anticoagulant was established by discontinuous polyacrylamide disc gel electrophoresis and by isotachophoresis. The anticoagulant enzyme is a single polypeptide chain without subunits having a molecular weight of 22,500. It consists of 28% aspartic acid residues and only 7% are basic amino acids. This agrees well with the fact that the anticoagulant is an acidic protein with an isoelectric point of 5.2. The anticoagulant is a proteolytic enzyme which hydrolyzes casein, fibrinogen and fibrin. The enzyme's optimum activity occurs around 55 degrees C. The anticoagulant showed no phospholipase A activity, low lethal activity, low hemorrhagic and capillary permeability activity, and no myotoxic activity.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000925:Anticoagulants / Q000302:isolation & purification*; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D010450:Endopeptidases / Q000302:isolation & purification* / Q000494:pharmacology; D005340:Fibrinogen / Q000378:metabolism; D005342:Fibrinolysis / Q000187:drug effects; D006461:Hemolysis / Q000187:drug effects; D007526:Isoelectric Point; D008970:Molecular Weight; D013379:Substrate Specificity; D014757:Viper Venoms / Q000032:analysis*
D000596:Amino Acids; D000925:Anticoagulants; D014757:Viper Venoms; D005340:Fibrinogen; D010450:Endopeptidases; C048743:cerastase F-4