Keratin decomposition by dermatophytes II. Presence of S-sulfocysteine and cysteic acid in soluble decomposition products

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Abstract
The dermatophyte Microsporum gypseum was grown on human hair in a mineral medium. Filtrates of cultures of various age were chromatographed on Sephadex gels and further characterized by chemical analysis and thin-layer chromatography. The products of keratin decomposition were separated into two fractions. The first fraction formed 10 to 20% of the bulk and contained proteins low in sulfur content. The second, very wide fraction contained oligopeptides and polypeptides with molecular weights from several hundreds up to approximately 13,000 with a peak at 1,000-2,000 daltons. This fraction contained a relatively high amount of cystine, S-sulfocysteine, and cysteic acid. S-sulfocysteine was present in the free state and also combined in peptides where its amount exceeded that of cystine. This supports the author's hypothesis on keratin decomposition by dermatophytes. According to this hypothesis, the fungus excretes sulfite which cleaves the disulfide bonds of keratin to cysteine and S-sulfocysteine. The substrate, denatured by sulfitolysis, is then more easily digestible by fungal proteases. Besides S-sulfocysteine, comparable amounts of cysteic acid were found in all analyses. This compound most probably originated by air oxidation of sulfur amino acids in the alkaline cultivation fluid.