Peroxidative crosslinking of myosins

V. Bhoite-Solomon, G. Kessler-Icekson, N. Shaklai*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


The effect of myoglobin, free hemin and H2O2 on myosins from heart and skeletal muscle was studied. SDS-gel electrophoresis revealed that each agent caused intermolecular thiol crosslinking of both myosins dissociable by excess of β-mercaptoethanol. In the simultaneous presence of H2O2 and myoglobin or H2O2 and free hemin, myosin formed covalent aggregates undissociable by β-mercaptoethanol and therefore assessed to formation of non S-S inter molecular covalent bonds. The latter aggregates are suggested to result from pairing of myosin radicals formed by the H2O2 induced ferryl iron state in myoglobin, free hemin or hemo-myosin.

Original languageEnglish
Pages (from-to)181-189
Number of pages9
JournalBiochemistry International
Issue number1
StatePublished - 1992


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