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)
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