| Autor: |
Kagan, Herbert M., Williams, Marcia A., Calaman, Susan D., Berkowitz, Ellen M. |
| Zdroj: |
Biochemical and Biophysical Research Communications; August 1983, Vol. 115 Issue: 1 p186-192, 7p |
| Abstrakt: |
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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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