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Deamination of protein lysyl ε-amino groups by peroxidase in vitro

✍ Scribed by M. A. Stahmann; A. K. Spencer

Publisher
Wiley (John Wiley & Sons)
Year
1977
Tongue
English
Weight
476 KB
Volume
16
Category
Article
ISSN
0006-3525

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✦ Synopsis

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.

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