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 semialdeh...

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Veröffentlicht in:Biochemical and biophysical research communications 1983-08, Vol.115 (1), p.186-192
Hauptverfasser: Kagan, Herbert M., Williams, Marcia A., Calaman, Susan D., Berkowitz, Ellen M.
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Sprache:eng
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Zusammenfassung: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 unidentitified prominent tritiated peak eluting near tyrosine as well as other lesser peaks, one of which is consistent with lysinonorleucine.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(83)90987-7