Histone H1 is a substrate for lysyl oxidase and contains endogenous sodium borotritide-reducible residues.
Incubation of purified bovine aortic lysyl oxidase with rat liver or calf thymus H1 histone results in the catalytic formation of hydrogen peroxide, indicating the substrate potential of H1 for this connective tissue enzyme. Sodium borotritide-reducible residues consistent with aminoadipic semialdehyde and the lysinonorleucine crosslinkage were generated in H1 by incubation with lysyl oxidase. H1 histone also contains endogenous reducible functions including an unidentified prominent tritiated peak eluting near tyrosine as well as other lesser peaks, one of which is consistent with lysinonorleucine.
D000594:Amino Acid Oxidoreductases / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001011:Aorta / Q000201:enzymology; D001894:Borohydrides / Q000494:pharmacology*; D002417:Cattle; D006657:Histones / Q000378:metabolism*; D007700:Kinetics; D008099:Liver; D008297:Male; D010084:Oxidation-Reduction; D008249:Protein-Lysine 6-Oxidase / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D013379:Substrate Specificity; D013950:Thymus Gland
D000596:Amino Acids; D001894:Borohydrides; D006657:Histones; C025364:sodium borohydride; D000594:Amino Acid Oxidoreductases; D008249:Protein-Lysine 6-Oxidase