Isozymes of glutamate dehydrogenase from oat leaves: Properties and light effect on synthesis

I. Barash; H. Mor; T. Sadon

Isozymes of glutamate dehydrogenase from oat leaves: Properties and light effect on synthesis

I. Barash^*, H. Mor, T. Sadon

^*Corresponding author for this work

School of Plant Sciences and Food Security

Research output: Contribution to journal › Article › peer-review

Abstract

Ammonium-dependent induction of a GDH isozyme in oat leaves was proportional to light intensity and inhibited by DCMU. The stimulation of GDH synthesis in response to ammonia was partially repressed by benzimidazole. The inducible (no. 1) and noninducible (no. 2) GDH isozymes wereseparated and purified by approximately 54 and 24 fold respectively. The two isozymes were highly specific for NAD and the rate of NADH oxidation was 7 to 9 times higher than NAD reduction. Both isozymes showed similar Km values for substrates of the reductive amination reaction and pH optima for NADH oxidation. The pH optima for NAD reduction were 9 and 8.2 for isozymes1 and 2 respectively. The two isozymes had a similar molecular weight, 2.2-2.4 × 10⁵ but differed in their isoelectric point and temperature sensitivity. Results suggest that the GDH isozymes in oat leaves are two different entities but might possess a similar metabolic function.

Original language	English
Pages (from-to)	493-500
Number of pages	8
Journal	Plant and Cell Physiology
Volume	17
Issue number	3
State	Published - Jun 1976

Cite this

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abstract = "Ammonium-dependent induction of a GDH isozyme in oat leaves was proportional to light intensity and inhibited by DCMU. The stimulation of GDH synthesis in response to ammonia was partially repressed by benzimidazole. The inducible (no. 1) and noninducible (no. 2) GDH isozymes wereseparated and purified by approximately 54 and 24 fold respectively. The two isozymes were highly specific for NAD and the rate of NADH oxidation was 7 to 9 times higher than NAD reduction. Both isozymes showed similar Km values for substrates of the reductive amination reaction and pH optima for NADH oxidation. The pH optima for NAD reduction were 9 and 8.2 for isozymes1 and 2 respectively. The two isozymes had a similar molecular weight, 2.2-2.4 × 105 but differed in their isoelectric point and temperature sensitivity. Results suggest that the GDH isozymes in oat leaves are two different entities but might possess a similar metabolic function.",

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T1 - Isozymes of glutamate dehydrogenase from oat leaves

T2 - Properties and light effect on synthesis

AU - Barash, I.

AU - Mor, H.

AU - Sadon, T.

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N2 - Ammonium-dependent induction of a GDH isozyme in oat leaves was proportional to light intensity and inhibited by DCMU. The stimulation of GDH synthesis in response to ammonia was partially repressed by benzimidazole. The inducible (no. 1) and noninducible (no. 2) GDH isozymes wereseparated and purified by approximately 54 and 24 fold respectively. The two isozymes were highly specific for NAD and the rate of NADH oxidation was 7 to 9 times higher than NAD reduction. Both isozymes showed similar Km values for substrates of the reductive amination reaction and pH optima for NADH oxidation. The pH optima for NAD reduction were 9 and 8.2 for isozymes1 and 2 respectively. The two isozymes had a similar molecular weight, 2.2-2.4 × 105 but differed in their isoelectric point and temperature sensitivity. Results suggest that the GDH isozymes in oat leaves are two different entities but might possess a similar metabolic function.

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Isozymes of glutamate dehydrogenase from oat leaves: Properties and light effect on synthesis

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