<b>PRODUCTION OF HUMAN GLICENTIN IN </b><i><b>ESCHERICHIA COLI</b></i>

Abstract

The gene encoding for human glicentin comprising 69 amino acid residues, a major form of gut glucagon, was designed and chemically synthesized based on the amino acid sequence deduced from the sequence of human preproglucagon. The gene was ligated to an expression vector pET-3a and expressed in Escherichia coli. The product thus obtained had an extra methionine at the N-terminus of glicentin molecule. Subsequently, the gene fragment encoding the first l0 amino acids of gene 10 protein of T7 phage (s10 peptide) was introduced into N-terminus of the glicentin gene to express a sl0-glicentin fusion protein. The treatment of the ensuing fusion protein with cathepsin C produced human glicentin successfully.