Peroxidative crosslinking of myosins
Bhoite-Solomon, V.; Kessler-Icekson, G.; Shaklai, N.
Biochemistry International 26(1): 181-189
1992
ISSN/ISBN: 0158-5231 PMID: 1616493 Document Number: 395305
The effect of myoglobin, free hemin and H2O2 on myosins from heart and skeletal muscle was studied. SDS-gel elecrophoresis revealed that each agent caused intermolecular thiol crosslinking of botymyosins dissociable by excess of .beta.-mercaptoethanol. In the simultaneous presence of H2O2 and myoglobin or H2O2 and free hemin, myosin formed covalent aggregates undissociable by .beta.-mercaptoethanol and therefore assessed to formation of non S-S intermolecular 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.