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Biochem Biophys Res Commun ; 200(3): 1735-41, 1994 May 16.
Artigo em Inglês | MEDLINE | ID: mdl-8185633

RESUMO

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.


Assuntos
Hormônio Paratireóideo , Sequência de Aminoácidos , Bioensaio , Humanos , Dados de Sequência Molecular , Hormônio Paratireóideo/química , Fragmentos de Peptídeos , Mapeamento de Peptídeos , Proteínas Recombinantes de Fusão/química
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