| Literature DB >> 11503514 |
S W Hwang1, J H Lee, H B Park, S H Pyo, J E So, H S Lee, S S Hong, J H Kim.
Abstract
A magainin derivative, designated MSI-344, was produced in Escherichia coli as fusion protein, by utilizing a truncated amidophsphoribosyltransferase of E. coli as a fusion partner. Bacterial cells transformed with the gene encoding the fusion protein were grown to a high cell density and induced with isopropyl-1-thio-b-D-galatoside (IPTG) to initiate product expression. The fusion protein was accumulated into cytoplasmic inclusion body and recombinant MSI-344 was released from the fusion partner by hydroxylamine treatment. Following cleavage of the fusion protein with hydroxylamine, the released MSI-344 was purified to homogeneity by cationic exchange chromatography. The final purity was at least 95% by reversed-phase high performance liquid chromatography (RP-HPLC). Purified recombinant MSI-344 was found to be indistinguishable from the synthetic peptide determined by amino acid sequences and antimicrobial activity assay.Entities:
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Year: 2001 PMID： 11503514 DOI： 10.1385/MB:18:3:193
Source DB: PubMed Journal: Mol Biotechnol ISSN： 1073-6085 Impact factor: 2.695