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Kinetic studies of glutamate dehydrogenase with glutamate and norvaline as substrates. Coenzyme activation and negative homotropic interactions in allosteric enzymes

The Biochemical Journal

Dec 1, 1969

Paul C Engel, K Dalziel

PMID: 4391040

Abstract

1. Kinetic studies of glutamate dehydrogenase were made with wide concentration ranges of the coenzymes NAD(+) and NADP(+) and the substrates glutamate and norvaline. Initial-rate parameters were evaluated. 2. Deviations from Michaelis-Menten behaviour towards higher activity were obser...read more

Mentioned in this Paper

Phosphate buffers
Enzymes, antithrombotic
Valerates
NADH
Enzymes for Treatment of Wounds and Ulcers
NADP
Enzymes, hematological
Glutamate
Enzymology
Hydrogen-Ion Concentration
Paper Details
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Kinetic studies of glutamate dehydrogenase with glutamate and norvaline as substrates. Coenzyme activation and negative homotropic interactions in allosteric enzymes

The Biochemical Journal

Dec 1, 1969

Paul C Engel, K Dalziel

PMID: 4391040

DOI:

Abstract

1. Kinetic studies of glutamate dehydrogenase were made with wide concentration ranges of the coenzymes NAD(+) and NADP(+) and the substrates glutamate and norvaline. Initial-rate parameters were evaluated. 2. Deviations from Michaelis-Menten behaviour towards higher activity were obser...read more

Mentioned in this Paper

Phosphate buffers
Enzymes, antithrombotic
Valerates
NADH
Enzymes for Treatment of Wounds and Ulcers
NADP
Enzymes, hematological
Glutamate
Enzymology
Hydrogen-Ion Concentration

Similar Papers Found In These Feeds

Solar-To-Chemical Conversion

This feed focuses on the latest research pertaining to mechanisms that facilitate reduction-oxidation biocatalysis only using light energy as a source. Here is the latest research.

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Paper Details
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  • Citations62
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