Temperature dependence of arginine kinase reaction in the tail muscle of live Sycionia ingentis as measured in vivo by 31P-NMR driven saturation transfer.
We have employed the driven 31P-NMR saturation transfer method to measure in vivo the temperature dependence of the forward and reverse unidirectional fluxes of the arginine kinase reaction in the tail muscle of a live shrimp, Sycionia ingentis. Our results indicated that neither the forward nor the reverse rate constants of this reaction were significantly temperature-dependent between 8 and 16 degrees C, in contrast to the kinetic characteristics of isolated arginine kinases.
Fan
T W
TW
Department of Land, Air and Water Resources, University of California, Davis 95616.
Higashi
R M
RM
Lane
A N
AN
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001122:Arginine Kinase / Q000378:metabolism*; D003445:Crustacea; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008962:Models, Theoretical; D009132:Muscles / Q000201:enzymology*; D010758:Phosphorus; D013696:Temperature
D010758:Phosphorus; D000255:Adenosine Triphosphate; D001122:Arginine Kinase