Cosolvent-induced aggregation inhibits myosin ATPase activity by stabilizing the predominant transition intermediate.

Abstract

High concentration of the cosolvent poly(ethylene glycol) (PEG) induces reversible aggregation of skeletal myosin subfragment 1 (S1) and inhibition of its Mg-ATPase activity [Highsmith et al. (1998) Biophys. J. 74, 1465-1472]. In the present work the effect of aggregation on the various steps of the ATPase cycle was studied. The isomerization and hydrolysis… (More)

Topics

Cite this paper

@article{Peyser2003CosolventinducedAI, title={Cosolvent-induced aggregation inhibits myosin ATPase activity by stabilizing the predominant transition intermediate.}, author={Y Michael Peyser and Shirley Shaya and Katalin Ajtai and Thomas P Burghardt and Andras Muhlrad}, journal={Biochemistry}, year={2003}, volume={42 43}, pages={12669-75} }