Abstract

Trimeresurus stejnegeri lectin (TSL) was expressed in the yeast Pichia pastoris under the control of alcohol oxidase (AOX1) promoter. The recombinant protein, which was glycosylated, can be purified by one-step affinity chromatography. The purified recombinant TSL shared similar sugar-binding activity and Specificity with the native protein as determined by hemagglutination and enzyme-linked lectin binding Assays.

Keywords: C-TYPE LECTIN, PICHIA PASTORIS, Trimeresurus stejnegeri lectin (TSL), alcohol oxidase (AOX1) promoter, galactose-binding C-type, mutagenesis, alcohol oxidase (AOX1)