-transparent.png){kind=logo}
A 31P nuclear magnetic resonance saturation transfer method was used to measure the temperature dependence of creatine kinase-catalysed fluxes in Langendorff-perfused rat hearts. A decrease in temperature from 37 to 4 degrees C lowered the observed steady-state fluxes by about 80%. These data were used in conjunction with calculated changes in substrate concentrations with temperature to estimate the activation energy for creatine kinase in situ. The apparent activation energy of 42 kJ/mol agrees reasonably well with the range of literature values for the enzyme in vitro. This demonstrates that the reaction is not diffusion-limited in situ and that extraction and dilution of the enzyme for study in vitro does not alter fundamental kinetic properties of the enzyme exhibited in the intact tissue.
P M Matthews, and
J L Bland, and
G K Radda
May 2002,
The Journal of biological chemistry,
P M Matthews, and
J L Bland, and
G K Radda
April 1996,
Physical review. D, Particles and fields,
P M Matthews, and
J L Bland, and
G K Radda
January 1990,
Anatomy and embryology,
P M Matthews, and
J L Bland, and
G K Radda
July 1973,
The Journal of biological chemistry,
P M Matthews, and
J L Bland, and
G K Radda
December 1998,
Biochimica et biophysica acta,
P M Matthews, and
J L Bland, and
G K Radda
June 1985,
Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.),
P M Matthews, and
J L Bland, and
G K Radda
June 1979,
Biochemical and biophysical research communications,
P M Matthews, and
J L Bland, and
G K Radda
January 1987,
Basic research in cardiology,
P M Matthews, and
J L Bland, and
G K Radda
March 1984,
Archives of biochemistry and biophysics,
P M Matthews, and
J L Bland, and
G K Radda
July 1992,
The Journal of biological chemistry,
