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- W1911768098 abstract "Peroxidase, catechol, and hydrogen peroxide were shown to react with proteins, causing a decrease in lysine detectable after acid hydrolysis. The loss of lysine did not occur in the presence of benzenesulfinic acid which suggested that the quinones formed by peroxidase had oxidized some lysyl residues to lysyl aldehyde that formed a cyclic ninhydrin negative Shiff's base. When peroxidase treated protein was oxidized with performic acid prior to hydrolysis a new ninhydrin positive compound was found, which was shown by cochromatography and mass spectroscopy to be α-aminoadipic acid. The α-aminoadipic acid recovered accounted for (20–40)% of the lysine lost." @default.
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- W1911768098 date "1977-06-01" @default.
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- W1911768098 title "Deamination of protein lysyl ɛ-amino groups by peroxidasein vitro" @default.
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- W1911768098 doi "https://doi.org/10.1002/bip.1977.360160610" @default.
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