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Highly purified preparations of glutamate dehydrogenase were obtained from mitochondrial and cytoplasmic fractions of rabbit liver by affinity chromatography on CL-Sepharose 4B modified by adenosine diphosphate. Some physico-chemical properties of the purified enzymes (e. g., specific activity, molecular weight, quaternary structure, stability against denaturating effect of urea, pH optimum of catalyzed reactions, Km values for substrates and coenzymes) were found to be identical. The sole difference was detected in the ability of enzyme preparations to be activated by adenosine diphosphate. The activation of the cytoplasmic enzyme is 160%, that of mitochondrial glutamate dehydrogenase is 230-240% under the same conditions.
R A Kazarian, and
S G Avetisian, and
L V Karabashian
February 1980,
Biokhimiia (Moscow, Russia),
R A Kazarian, and
S G Avetisian, and
L V Karabashian
September 1970,
The Journal of biological chemistry,
R A Kazarian, and
S G Avetisian, and
L V Karabashian
January 1980,
Prikladnaia biokhimiia i mikrobiologiia,
R A Kazarian, and
S G Avetisian, and
L V Karabashian
April 1985,
Journal of biochemistry,
R A Kazarian, and
S G Avetisian, and
L V Karabashian
June 1974,
Biochemical and biophysical research communications,
R A Kazarian, and
S G Avetisian, and
L V Karabashian
November 1978,
Biochimica et biophysica acta,
R A Kazarian, and
S G Avetisian, and
L V Karabashian
May 1975,
Comparative biochemistry and physiology. B, Comparative biochemistry,
R A Kazarian, and
S G Avetisian, and
L V Karabashian
September 1974,
The Journal of biological chemistry,
R A Kazarian, and
S G Avetisian, and
L V Karabashian
February 1974,
Acta medica Okayama,
R A Kazarian, and
S G Avetisian, and
L V Karabashian
January 1991,
Ukrainskii biokhimicheskii zhurnal (1978),
