Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.toxicon.2008.06.003
Title: Purification and N-terminal sequence of a serine proteinase-like protein (BMK-CBP) 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: 1-Aug-2008
Source: Gao, R., Zhang, Y., Gopalakrishnakone, P. (2008-08-01). Purification and N-terminal sequence of a serine proteinase-like protein (BMK-CBP) from the venom of the Chinese scorpion (Buthus martensii Karsch). Toxicon 52 (2) : 348-353. ScholarBank@NUS Repository. https://doi.org/10.1016/j.toxicon.2008.06.003
Abstract: A serine proteinase-like protein was isolated from the venom of Chinese red scorpion (Buthus martensii Karsch) by combination of gel filtration, ion-exchange and reveres-phase chromatography and named BMK-CBP. The apparent molecular weight of BMK-CBP was identified as 33 kDa by SDS-PAGE under non-reducing condition. The sequence of N-terminal 40 amino acids was obtained by Edman degradation. The sequence shows highest similarity to proteinase from insect source. When tested with commonly used substrates of proteinase, no significant hydrolytic activity was observed for BMK-CBP. The purified BMK-CBP was found to bind to the cancer cell line MCF-7 and the cell binding ability was dose-dependent. © 2008 Elsevier Ltd. All rights reserved.
Source Title: Toxicon
URI: http://scholarbank.nus.edu.sg/handle/10635/67245
ISSN: 00410101
DOI: 10.1016/j.toxicon.2008.06.003
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