Please use this identifier to cite or link to this item: https://doi.org/10.1007/978-3-540-69139-6-206
Title: A novel trypsin-like serine proteinase from the venom of the Chinese scorpion Buthus martensii Karsch
Authors: Gao, R. 
Zhang, Y. 
Gopalakrishnakone, P.
Keywords: Cell binding
Purification
Scorpion venom
Serine proteinase
Issue Date: 2008
Source: Gao, R.,Zhang, Y.,Gopalakrishnakone, P. (2008). A novel trypsin-like serine proteinase from the venom of the Chinese scorpion Buthus martensii Karsch. IFMBE Proceedings 21 IFMBE (1) : 829-832. ScholarBank@NUS Repository. https://doi.org/10.1007/978-3-540-69139-6-206
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.
Source Title: IFMBE Proceedings
URI: http://scholarbank.nus.edu.sg/handle/10635/74820
ISBN: 9783540691389
ISSN: 16800737
DOI: 10.1007/978-3-540-69139-6-206
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