PMID: 6020042Apr 7, 1967Paper

Heat inactivation of the relaxing site of actomyosin: prevention and reversal with dithiothreitol

Science
H M LEVY, E M RYAN

Abstract

Adenosine triphosphate and magnesium (MgATP) inhibit contraction by binding to a specific relaxing site on natural actomyosin gel. This inhibitory control site is distinct from the active sites where MgATP causes contraction. In high concentrations of MgATP, calcium triggers contraction by releasing the protein from substrate inhibition, allowing the contractile reactions to occur. Heating the protein for 5 minutes at 43 degrees C selectively inactivates the relaxing site. After this treatment, actomyosin with MgATP contracts as well without calcium as with it. That this effect of heat is prevented and reversed by dithiothreitol (an agent that reduces disulfide bonds) indicates that the structure of the relaxing site depends on certain labile sulfhydryl groups, which may be those of tropomyosin. When these are oxidized to disulfide bonds, the site loses its activity; when the disulfide bonds are reduced, the site regains its activity.

References

Jul 1, 1965·Journal of Biochemistry·S Ebashi, A Kodama
Aug 1, 1958·Archives of Biochemistry and Biophysics·S EBASHI
Sep 1, 1960·Archives of Biochemistry and Biophysics·Y TONOMURA, J YOSHIMURA
Apr 1, 1964·Biochemistry·W W CLELAND
Aug 8, 1964·Nature·S EBASHI, F EBASHI
Aug 1, 1962·Archives of Biochemistry and Biophysics·K LAKID R KOMINZ

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Citations

Apr 20, 1972·Biochimica Et Biophysica Acta·D J HartshorneF Fuchs
Nov 1, 1967·The Journal of General Physiology·H M Levy, E M Ryan
May 1, 1968·The Journal of General Physiology·F Fuchs, F N Briggs
Apr 1, 1970·Archives of Biochemistry and Biophysics·T FukazawaW F Mommaerts

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