Peroxidative crosslinking of myosins.
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 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 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.
Bhoite-Solomon
V
V
Sackler Institute of Molecular Medicine, Sackler Faculty of Medicine, Tel-Aviv University, Israel.
Kessler-Icekson
G
G
Shaklai
N
N
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D006168:Guinea Pigs; D006427:Hemin / Q000737:chemistry / Q000494:pharmacology*; D006861:Hydrogen Peroxide / Q000737:chemistry / Q000494:pharmacology*; D008623:Mercaptoethanol / Q000494:pharmacology; D009132:Muscles / Q000737:chemistry; D009206:Myocardium / Q000737:chemistry; D009211:Myoglobin / Q000737:chemistry / Q000494:pharmacology*; D009218:Myosins / Q000737:chemistry*
D009211:Myoglobin; D008623:Mercaptoethanol; D006427:Hemin; D006861:Hydrogen Peroxide; D009218:Myosins