Glutamate dehydrogenase concentration as a determinant in the effect of purine nucleotides on enzymatic activity.
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Adenine Nucleotides↗
Biomedical subjects
C Frieden
Publications and source records attributed to C Frieden.
On the role of amino groups in the structure and function of glutamate dehydrogenase. I. Effect of acetylation on catalytic and regulatory properties.
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Acetates↗
On the role of amino groups in the structure and function of glutamate dehydrogenase. II. Effect of acetylation on molecular properties.
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Acetates↗
Cooperative interaction between the GTP binding sites of glutamate dehydrogenase.
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Chemical Phenomena↗
Myoadenylate deaminase deficiency.
Myoadenylate deaminase (adenosine monophosphate deaminase--AMPDA) was recently shown to be deficient in a group of patients by use of a histochemical and biochemical method based on the elaboration of ammonia by this enzyme as it deaminates 5' AMP. We have confirmed the utility of this histochemical method and the existence of persons deficient in AMPDA through the use of an unrelated assay technique. The lack of enzyme activity is not associated with any inhibitory activity in the muscles of patients with this disorder. The clinical diversity of these patients suggests that this lack may represent a normal variant or a subclinical state rather than an actual disease. The occurrence of AMPDA deficiency in both sexes points to possible autosomal inheritance.
AMP Deaminase↗