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1. Kinetic aspects of the reaction between crystalline bovine liver glutamate dehydrogenase and formiminoglutamate were investigated to establish the conditions under which the latter may interfere with the assay of glutamate by using glutamate dehydrogenase and to explain why formiminoglutamate accumulates in vivo after histidine loading, although it can react with glutamate dehydrogenase. The Km and Vmax. values were compared with those of the enzyme reacting with glutamate. At pH 7.4 Km for formiminoglutamate was much higher and Vmax. much lower than the values for glutamate. 2. The equilibrium constant at pH 7.0 was 0.017 micrometer with formiminoglutamate, i.e. about one two-hundredths that with glutamate. 3. In vivo the interaction between glutamate dehydrogenase and formiminoglutamate is minimal even when the concentration of the latter in the liver is greatly raised, as in cobalamine or folate deficiency after histidine loading. 4. At pH 9.3, i.e. under the conditions for the assay of glutamate by glutamate dehydrogenase, formiminoglutamate reacts readily with the enzyme.
J Vińa, and
R Hems, and
H A Krebs
January 1976,
Advances in protein chemistry,
J Vińa, and
R Hems, and
H A Krebs
July 1983,
Biokhimiia (Moscow, Russia),
J Vińa, and
R Hems, and
H A Krebs
June 2007,
FEBS letters,
J Vińa, and
R Hems, and
H A Krebs
October 1971,
Klinische Wochenschrift,
J Vińa, and
R Hems, and
H A Krebs
January 1978,
Biophysical chemistry,
J Vińa, and
R Hems, and
H A Krebs
September 1970,
European journal of biochemistry,
J Vińa, and
R Hems, and
H A Krebs
June 1982,
European journal of biochemistry,
J Vińa, and
R Hems, and
H A Krebs
July 1972,
The Biochemical journal,
J Vińa, and
R Hems, and
H A Krebs
January 1971,
Zeitschrift fur die gesamte experimentelle Medizin einschliesslich experimentelle Chirurgie,
J Vińa, and
R Hems, and
H A Krebs
January 1985,
Methods in enzymology,
