Purification and characterization of a rhamnose-binding lectin with immunoenhancing activity from grass carp (Ctenopharyngodon idellus) ovaries

被引：42

作者：

Lam, YW ^{[1
]}

Ng, TB ^{[1
]}

机构：

[1] Chinese Univ Hong Kong, Dept Biochem, Fac Med, Shatin, Hong Kong, Peoples R China

来源：

PROTEIN EXPRESSION AND PURIFICATION | 2002年 / 26卷 / 03期

关键词：

grass carp; lectin; rhamnose-binding;

D O I：

10.1016/S1046-5928(02)00559-4

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

A rhamnose-specific lectin was isolated from ovaries of the grass carp (Ctenopharyngodon idellus). The grass carp lectin possesses a molecular mass of 205 kDa. It is composed of six subunits each with a molecular mass of 35 kDa. The N-terminal amino acid sequence of the grass carp shows similarity to those of other fish species with 26-35% amino acid identity. It is mitogenic toward murine splenocytes and peritoneal exudate cells. (C) 2002 Elsevier Science (USA). All rights reserved.

引用

页码：378 / 385

页数：8

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