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

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.