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Cross linking of proteins in vitro by peroxidase

✍ Scribed by M. A. Stahmann; A. K. Spencer; G. R. Honold

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

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✦ Synopsis

Abstract

The enzyme peroxidase, a substrate (hydrogen donor), and hydrogen peroxide aggregated and polymerized soluble proteins included in the reaction mixture. Gel filtration and acrylamide disk gel electrophoresis revealed newly formed dimers, trimers, and higher protein polymers. Some of the protein polymers withstood the denaturing conditions of dodecyl sulfate disk gel electrophoresis; thus the formation of some covalent cross links was indicated. It is suggested that peroxidase catalyzes the oxidation of hydrogen donors to form free radicals or quinones, which subsequently interact with, cross link, and alter the soluble proteins.

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