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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| Authors: | A M A Nascimento H R T Souza M S Xavier J E Thiemann L Vilela M Mares-Guia |
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| Institution: | (1) Departemento de Biologia Geral, UFMG, Caixa Postal 486, 31270-901 Belo Horizonte, MG, Brazil;(2) Departamento de Bioquímica e Imunologia, UFMG, Caixa Postal 486, 31270-901 Belo Horizonte, MG, Brazil;(3) Biobras S.A, Distrito Industrial, 39.404-004 Montes Claros, MG, Brazil |
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| Abstract: | Summary 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. |
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