| Literature DB >> 8185633 |
S Nakagawa1, Y Tamakashi, Y Ishibashi, M Kawase, S Taketomi, O Nishimura, T Fukuda.
Abstract
The production of hPTH(1-34) by site specific chemical cleavage of [Cys35]hPTH(1-84) obtained by a biotechnology technique is described. The amino-peptide bond of S-cyanylated cysteine residues in peptides or proteins is specifically cleaved by exposure to an alkaline solution (Stark, G. R. (1977) Methods Enzymol, 47, 129-132). However, when applying this method to [Cys35]hPTH(1-84), we observed many by-products. Formation of these by-products was suppressed using a short reaction in 0.03N NaOH containing 6M urea at low temperature, and hPTH(1-34) was specifically produced. The product was indistinguishable from standard hPTH(1-34) with respect to chemical and biological characterization.Entities:
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Year: 1994 PMID: 8185633 DOI: 10.1006/bbrc.1994.1653
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575