PMID: 6107126Nov 5, 1980Paper

Steady-state magnesium ion-adenosine triphosphatase activities of myosin and its subfragment 1 derivative

Biochimica Et Biophysica Acta
L H Schliselfeld

Abstract

The Mg2+-ATPase activity of myosin and its subfragment 1 (ATP phosphohydrolase, EC 3.6.1.3) always followed normal Michaelis-Menten kinetics for ATP concentrations less than 10 microM. The average Km values at pH 7.4 and 25 degrees C are 0.33 +/- 0.04 microM for myosin and 0.43 +/- 0.11 microM for subfragment 1. At low salt concentration myosin yields a second hyperbolic increase in Mg2+-ATPase activity as the ATP rises from 10.2 microM to 153 microM: V doubles with a Km of 11 +/- 5 microM. This second low-salt-dependent increase in Mg2+-ATPase activity occurred between pH 6.8 and pH 8.7. It was not affected by the presence of 0.10 M EGTA to remove Ca2+ contamination. Solubilization of the catalytic sites by assaying myosin for ATPase activity in the presence of 0.60 M NaCl or by conversion of myosin to subfragment 1 eliminated the secondary hyperbolic increase. Subfragment 1 has a significantly different pH-activity curve from that of myosin. Subfragment 1 has an activity peak at pH 6.0, a rising activity as the pH goes from 8.7 to 9.8, and a deep activity valley between pH 6.8 and pH 8.4. Myosin has a very shallow trough of activity at pH 6.8 to 8.4, and in 1.0 mM ATP its activity drops as the pH decreases from 6.8 to 6.0. Na...Continue Reading

References

Aug 12, 1976·Biochimica Et Biophysica Acta·L H Schliselfeld
Dec 1, 1975·Canadian Journal of Biochemistry·T Nihei, C A Filipenko
Mar 15, 1977·FEBS Letters·R S Taylor, A G Weeds
May 1, 1976·Quarterly Reviews of Biophysics·D R TrenthamC R Bagshaw
Sep 1, 1967·European Journal of Biochemistry·M BárányM Goffart
Sep 1, 1968·Biochemistry·L H Schliselfeld, M Bárány
Feb 11, 1967·Nature·K Bárány, H Oppenheimer
Aug 1, 1953·The Biochemical Journal·M DIXON

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Citations

Apr 27, 2010·Meat Science·Marie YamazakiDarl R Swartz
Dec 1, 1986·European Journal of Biochemistry·J J BechetA d'Albis

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