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KMID : 0380219990320060579
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Journal of Biochemistry and Molecular Biology
1999 Volume.32 No. 6 p.579 ~ p.584
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Purification and Characterization of a Novel Serine Protease with Fibrinolytic Activity from Tenodera sinensis (Chinese Mantis) Egg Cases
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Cho So-Yean
Hahn Bum-Soo
Kim Yeong-Shik
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Abstract
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Mantis egg fibrolase (MEF-3) was purified from the egg cases of Tenodera sinensis using ammonium sulfate fractionation, gel filtration on Bio-Gel P-60, DEAE Affi-Gel blue gel affinity chromatogragphy, and MONO-Q anion-exchange chromatography. This protease had a molecular weight of 35,600 Da as determined by SDS-polyacrylamide gel electrophoresis under reducing conditions and its isoelectric point was 6.0. The N-terminal amino acids sequence was Ala-Thr-Gln-Asp-Asp-Ala-Pro-Pro-Gly-Leu-Ala-Arg-Arg. This sequence was 80% homologous to the serine protease from Tritirachium album. MEF-3 readily digested the α-and β-chains of fibrinogen and more slowly the γ-chains. It showed strong proteolytic and fibrinolytic activities. Phenylmethanesulfonyl fluoride and chymostatin inhibited its proteolytic activity, while EDTA, EGTA, cysteine, β-mercaptoethanol, elastinal, tosyl-lysine chloromethylketone, and tosyl-amido-2-phenylethyl chloromethyl ketone did not affect its proteolytic activity. Among the chromogenic protease substrates, the most sensitive one to the hydrolysis of MEF-3 was benzoyl-Phe-Val-Arg-p-nitroanilide. Based on these experimental results, we speculated that MEF-3 is a serine protease with a strong fibrin(ogen)olytic activity.
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KEYWORD
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Fibrinolytic activity, Properties, Purification, Serine protease, Tenodera sinensis
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