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KMID : 0380219930260040363
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Journal of Biochemistry and Molecular Biology
1993 Volume.26 No. 4 p.363 ~ p.369
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Purification and Characterization of a Fibrinolytic Enzyme from Korean Snake(Agkistrodon halys) Venom
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Kwang-Heo Chung and Doo-Sik Kim
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Abstract
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A fibrinolytic enzyme was purified to homogeneity from the venom of Korean Salmosa snake Agkistrodon halys by a combination of benzamidine-Sepharose affinity chroma-tography and FPLC Mono Q ion exchange fractionation. The purified enzyme is a glycoprotein and migrates as a single band with molecular mass of 51,000 Da on SDS-polyacrylamide gel electrophoresis. The native molecular weight was determined to be 52,000 Da by FPLC gel filtration. The fibrinolytic enzyme is characterized by its isoelectric point of 3.52. Amino terminal sequence of the enzyme was identified to be Val-Ile-Gly-Gly-Asp-Glu-Asn-Ile-Asn-Glu-His-Arg-Phe-Leu-Val-Ala-Met, which is homologous to that of protein C activator from Agkistrodon contortrix.
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