Abstract
Improved growth conditions were developed for normal strain 1A of Neurospora crassa in order to induce a high level of the NAD-specific glutamate dehydrogenase. A simplified purification procedure is described in order to obtain the enzyme in high yield and specific activity. The homogeneous enzyme has a molecular weight of 480,000 ± 27,000 by sedimentation equilibrium analysis, and is dissociable into four identical subunits of 116,000 ± 5,400 molecular weight. The amino acid composition of the enzyme was determined. Isophthalate was found to be a strong competitive inhibitor and an effective stabilizer of the enzyme. The molecular properties indicate that the subunit structure of this enzyme differs substantially from those of the glutamate dehydrogenases from vertebrates and of the NADP-specific enzyme from Neurospora.
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