Isolation and partial characterization of the Asp-B10, Tyr-B25-des-(B26-B30)-proinsulin analog from inclusion bodies in Escherichia coli
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A proinsulin analog constructed by site-directed mutagenesis was expressed as a fusion protein that formed inclusion bodies inside the cells. It was purified from the isolated inclusion bodies and proinsulin was obtained by trifluoro-acetic acid, dimethyl sulfoxide and hydrochloric acid cleavage. The released proinsulin analog was confirmed by its molecular weight as determined by SDS-PAGE.
KeywordsEscherichia Coli Molecular Weight Dimethyl Fusion Protein Hydrochloric Acid
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