Peroxidative crosslinking of myosins.

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