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The time-resolved and steady state fluorescence properties were measured for pig heart cytoplasmic malate dehydrogenase at pH 6.0 and 8.0. The fluorescence decay can be described by two rate processes, according to the functions: I(t) = 0.7e(-t/1.0) + 0.3e(-t/4.4) for the free enzyme and I(t) = 0.7e(-t/0.8) + 0.3e(-t/2.0 for the enzyme . NADH complex. Quenching by NADH of the tryptophan fluorescence is linear. The only effect of pH is to change the association constant for NADH binding; the fluorescence of the free enzyme and the fluorescence quenching by NADH, I-, and acrylamide are unaffected by pH. Thus there are no changes in conformation of the free enzyme or of the NADH complex over the range of pH 6 to 8.
T Torikata, and
L S Forster, and
R E Johnson, and
J A Rupley
March 1975,
The Journal of biological chemistry,
T Torikata, and
L S Forster, and
R E Johnson, and
J A Rupley
July 1975,
Biochemistry,
T Torikata, and
L S Forster, and
R E Johnson, and
J A Rupley
December 1970,
Biochemical and biophysical research communications,
T Torikata, and
L S Forster, and
R E Johnson, and
J A Rupley
December 1968,
The Journal of biological chemistry,
T Torikata, and
L S Forster, and
R E Johnson, and
J A Rupley
November 1970,
European journal of biochemistry,
T Torikata, and
L S Forster, and
R E Johnson, and
J A Rupley
January 2014,
Journal of fluorescence,
T Torikata, and
L S Forster, and
R E Johnson, and
J A Rupley
April 1966,
Nature,
T Torikata, and
L S Forster, and
R E Johnson, and
J A Rupley
May 1975,
The Journal of biological chemistry,
T Torikata, and
L S Forster, and
R E Johnson, and
J A Rupley
January 2014,
Journal of fluorescence,
T Torikata, and
L S Forster, and
R E Johnson, and
J A Rupley
February 1989,
Biochimica et biophysica acta,
