Cystine and cysteine analysis as the same phenylthiocarbamyl derivatives by HPLC in protein hydrolyzates

I. Molnár-Perl, M. Morvai

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

A new approach is described, and a novel explanation presented, for the high performance liquid chromatographic analysis of cystine and cysteine as their phenylthiocarbamyl derivatives. PTC cystine and cysteine have been eluted with the same retention times and molar responses, most probably due to electrophilic attack of phenylisothiocyanate on cystine resulting in the scission of the disulfide bond yielding two moles of cysteine. Further, total PTC cystine and cysteine have been measured both in model solutions and in standard protein hydrolyzates (lysozyme, bovine albumin, ribonuclease) with the same linearity as the other ineteen amino acids. The reproducibility of the measurements, at the 250-750 pmole level, proved to be 4.1% (Relative Standard Deviation %) or less.

Original languageEnglish
Pages (from-to)132-136
Number of pages5
JournalChromatographia
Volume34
Issue number3-4
DOIs
Publication statusPublished - Aug 1 1992

Keywords

  • Column liquid chromatography
  • Cysteine, cystine
  • Phenylthiocarbamyl derivatives
  • Protein hydrolyzates

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Clinical Biochemistry
  • Organic Chemistry

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