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pubmed-article:1422224pubmed:abstractTextGene fusion has been used to produce the cytoplasmic domain of an endocytic receptor. DNA sequences coding for the 52 COOH-terminal amino acids of the mannose receptor from human macrophages, including the 41-amino acid cytoplasmic tail, were fused to the codons specifying the carbohydrate-recognition domain (CRD) of rat mannose-binding protein. The fusion protein was expressed in Escherichia coli and purified in one step on mannose-Sepharose, making use of the carbohydrate-binding activity of the CRD. The tail peptide was released from the fusion protein using endoproteinase Arg-C. This method provides an alternative to chemical synthesis for the production of midlength peptides.lld:pubmed
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pubmed-article:1422224pubmed:articleTitleExpression and purification of the cytoplasmic tail of an endocytic receptor by fusion to a carbohydrate-recognition domain.lld:pubmed
pubmed-article:1422224pubmed:affiliationDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032.lld:pubmed
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pubmed-article:1422224pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed