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Purification and characterization of a rhamnose-binding lectin with immunoenhancing activity from grass carp
1Department of Biochemistry, Faculty of Medicine, Basic Medical Sciences Bldg. Rm. 302B, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong, China.
Protein Expression and Purification
|December 4, 2002
Abstract:
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.
