A novel trypsin-like serine proteinase from the venom of the Chinese scorpion Buthus martensii Karsch

Abstract

By using the combination of gel filtration, ion-exchange and reveres-phase chromatography, a novel trypsinlike serine proteinase was isolated from the venom of Buthus martensii Karsch and named BMK-CB. The apparent molecular weight of BMK-CB was identified as 32 kDa by SDSPAGE. The N-terminal sequence of 40 amino acids was obtained by Edman degradation. The sequence shows highest similarity to proteinase from insect source. The purified BMKCB was found to bind to the cancer cell line MCF-7 and the cell binding ability was dose-dependent. To our knowledge, BMK-CB forms the first trypsin-like serine proteinase from the scorpion venom. © 2008 Springer-Verlag.