| Literature DB >> 7044895 |
R Wetzel, D G Kleid, R Crea, H L Heyneker, D G Yansura, T Hirose, A Kraszewski, A D Riggs, K Itakura, D V Goeddel.
Abstract
A gene has been constructed which codes for an analog of human proinsulin in which the normal 35-amino acid connecting peptide is replaced by a "mini-C" peptide of six amino acids (Arg-Arg-Gly-Ser-Lys-Arg). The gene, composed of oligonucleotide fragments synthesized by the triester method, was cloned and expressed as a beta-galactosidase hybrid protein. The proinsulin analog was separated from beta-galactosidase by cyanogen bromide cleavage and purified. Controlled disulfide exchange in the S-sulfonate of the analog generated a molecule having high-pressure liquid chromatography (HPLC) and radioimmunoassay (RIA) behavior consistent with a proinsulin-like structure.Entities:
Mesh：
Substances：
Year: 1981 PMID： 7044895 DOI： 10.1016/0378-1119(81)90061-5
Source DB: PubMed Journal: Gene ISSN： 0378-1119 Impact factor: 3.688