PMID: 1213670Oct 1, 1975Paper

Reduction of S-sulpho groups by tributylphosphine: an improved method for the recombination of insulin chains

Hoppe-Seyler's Zeitschrift für physiologische Chemie
U T Rüegg, H G Gattner

Abstract

All 4 S-sulpho groups of the S-sulpho substituted insulin A-chain could be removed with 4 mol of tributylphosphine. Reduction of a 1:1 mixture of both S-sulpho insulin chains with tributylphosphine followed by air oxidation gave insulin which was isolated in pure form and high yield. Removal of excess reducing agent was not necessary, in contrast to the usual procedures employing thiols for the reduction step. This constitutes a rapid and simple method for the generation of insulin from its chains. A new method for the purification of S-sulpho-A-chain has been developed.

Citations

Sep 2, 2000·Journal of Peptide Science : an Official Publication of the European Peptide Society·R Söll, A G Beck-Sickinger
Feb 1, 1995·International Journal of Peptide and Protein Research·I MaugrasR Nyfeler
Aug 1, 1997·The Journal of Peptide Research : Official Journal of the American Peptide Society·A BernhardtM Schutkowski
Dec 1, 1982·Hoppe-Seyler's Zeitschrift für physiologische Chemie·R KnorrC R Kahn
Mar 1, 1990·International Journal of Peptide and Protein Research·G B Fields, R L Noble
Nov 1, 1983·Hoppe-Seyler's Zeitschrift für physiologische Chemie·R KnorrC R Kahn
Feb 1, 1979·International Journal of Peptide and Protein Research·R C Paynovich, F H Carpenter
Nov 28, 2017·Journal of Medicinal Chemistry·Kateřina MacháčkováJiří Jiráček

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