The effect of hydrostatic pressure on the interaction of actomyosin subfragment 1 with nucleotides.
Increased hydrostatic pressure has previously been shown to reduce the tension of isometrically contracting skinned muscle fibres. An isomerization of the actomyosin complex is known to be pressure sensitive, but the pressure sensitivity of other steps in the ATPase pathway has not been characterised. We report here the effect of pressure on the ATP hydrolysis step of the myosin subfragment 1 ATPase, ADP binding to actomyosin subfragment 1 and the rate of ATP induced dissociation of actomyosin subfragment 1. We discuss the relationship of these changes to the observed effect of pressure on skinned muscle fibres.
McKillop
D F
DF
Department of Biochemistry, University of Bristol, U.K.
Geeves
M A
MA
Balny
C
C
D000205:Actomyosin / Q000378:metabolism*; D000244:Adenosine Diphosphate / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism*; D006874:Hydrostatic Pressure; D007700:Kinetics; D011485:Protein Binding; D013053:Spectrophotometry
D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D000205:Actomyosin; D000251:Adenosine Triphosphatases