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. 1966 Aug;100(2):309–314. doi: 10.1042/bj1000309

Spectrophotometric measurement of the liberation of the α-amino group of cysteine residues in polypeptides

S Streichman 1, Y Avi-Dor 1
PMCID: PMC1265137  PMID: 16742406

Abstract

1. The reaction between β-bromopyruvic acid and SH groups of cysteine residues in reduced ribonuclease and in some other polypeptides was investigated. 2. One molecule of the acid was found to be necessary to block one SH group in reduced ribonuclease. The stoicheiometry of the interaction and the spectral characteristics of the compound formed suggested that the product is and S-oxalomethyl (R·S·CH2·CO·CO2H) derivative of reduced ribonuclease. 3. Digestion of reduced S-oxalomethylated ribonuclease by trypsin or chymotrypsin induced changes in the spectrum that could be attributed to the liberation of the α-amino group of S-oxalomethylated cysteine residues from peptide bonds. The spectral changes that accompanied the hydrolysis of specific peptide bonds in reduced S-oxalomethylated ribonuclease and S-oxalomethylated co-poly(l-Lys,l-CySH) allowed the kinetics of the digestion to be followed. 4. Possible applications of the spectrophotometric method in the study of protein structure are discussed.

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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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