Abstract
Chromatographic systems for cystine peptides were established and mixed disulfide formation was studied using a Technicon Amino Acid Analyzer. The ninhydrin molar color yields of peptides with N-terminal cystine was increased by splitting the disulfide bond with sodium bisulfite. Cystine peptides were prepared in the sulfhydryl form by reducing the disulfide bonds with dithiothreitol. The reduced peptides were separated from dithiothreitol on a small column of Dowex 50W X4 in the H + form. The sulfhydryl peptides were mixed together and allowed to oxidize completely. The oxidized products were analyzed in the chromatographic system. The formation of symmetrical and mixed disulfides from the sulfhydryl compounds appeared to occur randomly.
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