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Title: Actin binding to cross-linked 10 S smooth muscle myosin and 9 S heavy meromyosin. Author: Sohma H. Journal: Biochem Int; 1992 Aug; 27(4):699-707. PubMed ID: 1417903. Abstract: Unphosphorylated gizzard myosin and heavy meromyosin were cross linked in the 10 S and 9 S states, respectively, by the cleavable cross linker, 3,3'-dithiobis (sulfosuccinimidyl-propionate) (DTSSP). The 10 S to 6 S transition for cross-linked 10 S myosin appeared to cease; myosin appeared to remain in the 10 S state from measurements of viscosity and Mg(2+)-ATPase activity. The loss of the transition for cross-linked 9 S heavy meromyosin (HMM) was also indicated by Mg(2+)-ATPase activity. The cross links were cleaved by incubation with 50 mM dithiothreitol. From direct binding measurements, the estimated Kd's of actin to cross-linked and control heavy meromyosin were 167 and 16 microM, respectively. The binding affinity of cross-linked HMM to actin was restored to the control level by dithiothreitol.[Abstract] [Full Text] [Related] [New Search]