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Functional Expression of a Galactose-Binding C-Type Lectin In Pichia pastoris

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

Document Type: Review Article

Publication date: 01 June 2001

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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