Purification and N-terminal sequence of a serine proteinase-like protein (BMK-CBP) from the venom of the Chinese scorpion (Buthus martensii Karsch)

被引：33

作者：

Gao, Rong ^{[2
]}

Zhang, Yong ^{[1
,2
]}

Gopalakrishnakone, Ponnampalam ^{[3
]}

机构：

[1] Natl Univ Singapore, Fac Engn, Div Bioengn, Singapore 117576, Singapore

[2] Natl Univ Singapore, Nanosci & Nanotechnol Initiat, Singapore 117576, Singapore

[3] Natl Univ Singapore, Fac Med, Dept Anat, Singapore 117597, Singapore

来源：

TOXICON | 2008年 / 52卷 / 02期

关键词：

scorpion venom; serine proteinase; purification; cell binding;

D O I：

10.1016/j.toxicon.2008.06.003

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

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 protemase, 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. (C) 2008 Elsevier Ltd. All rights reserved.

引用

页码：348 / 353

页数：6

共 23 条

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