Purification and properties of a fibrinogenase from the venom of Naja nigricollis |
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Authors: | Herbert J Evans |
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Institution: | Department of Biochemistry, Medical College of Virginia, Virginia Commonwealth University, Richmond, VA 23298, U.S.A. |
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Abstract: | A fibrinogenolytic proteinase from the venom of Naja nigricollis was purified by chromatography on Bio-Rex 70 and Phenyl-Sepharose. The purified enzyme, designated proteinase F1, was homogeneous by the criterion of SDS-polyacrylamide gel electrophoresis, and consisted of a single chain with a molecular weight of 58 000. Purified proteinase F1 had approximately 15-fold more proteinase activity than the crude venom, based on its ability to inactive α2-macroglobulin. The enzyme acted on only the Aα-chain of fibrinogen and left the Bβ- and γ-chains intact. The pH optimum for this fibrinogenolytic activity was in the range of pH 8 to 10. In addition to its activity on fibrinogen, proteinase F1 was active on α2-macroglobulin and fibronectin, but did not degrade casein, hemoglobin or bovine serum albumin. The enzyme was not inhibited by inhibitors of serine proteinases, cysteine proteinases or acid proteinases, but only by the metalloproteinase inhibitor, EDTA. The inhibition by EDTA could be prevented by Zn2+, but not by Ca2+ or Mg2+. |
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Keywords: | Fibrinogenase Snake venom (N nigricollis) SDS sodium dodecyl sulfate BAEE BTEE BAPNA |
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