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. 1981 Oct 1;199(1):61–67. doi: 10.1042/bj1990061

Modification by simetryn sulphoxide of a specific thiol group in rat haemoglobin.

G J Hughes, C de Jong, R W Fischer, K H Winterhalter, K J Wilson
PMCID: PMC1163334  PMID: 7337714

Abstract

Native rat haemoglobins were found to bind simetryn sulphoxide to an extent 40-fold greater than human haemoglobin. This specific behaviour was studied by using only high-pressure ('performance') liquid chromatography for the preparative separation of globin chains and the isolation of peptides resulting from chemical and enzymic degradation. High recoveries (greater than 80%) of peptides throughout the procedures in combination with microsequence techniques, allow a definitive assignment of the residue undergoing modification. The haemoglobin beta-chain cystine-125 residue, with a stoichiometry of one per tetramer of rat haemoglobin, was found to be modified. Stereochemical implications of this finding are discussed. Simetryn sulphoxide would appear to be useful as a specific reagent for the mapping of exposed thiol residues in proteins.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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