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Cross linking of proteins in vitro by peroxidase
Author(s) -
Stahmann M. A.,
Spencer A. K.,
Honold G. R.
Publication year - 1977
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1977.360160611
Subject(s) - chemistry , peroxidase , hydrogen peroxide , gel electrophoresis , size exclusion chromatography , covalent bond , polymerization , substrate (aquarium) , radical , polyacrylamide gel electrophoresis , polymer , acrylamide , sodium dodecyl sulfate , monomer , polymer chemistry , enzyme , biochemistry , chromatography , organic chemistry , oceanography , geology
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.