BMB Reports
- Volume 32 Issue 6
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- Pages.579-584
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- 1999
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- 1976-670X(eISSN)
Purification and Characterization of a Novel Serine Protease with Fibrinolytic Activity from Tenodera sinensis (Chinese Mantis) Egg Cases
- Cho, So-Yean (Natural Products Research Institute, Seoul National University) ;
- Hahn, Bum-Soo (Natural Products Research Institute, Seoul National University) ;
- Kim, Yeong-Shik (Natural Products Research Institute, Seoul National University)
- Published : 1999.11.30
Abstract
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