Hepatic damage and glutamate oxaloacetate transaminase elevations during fetal asphyxia

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Effects of Vitamin B6 on the Brain Glutamate Pyrovate Transaminase and Glutamate Oxaloacetate Transaminase in Young and Old Rats

Excessive amounts of extracellular glutamate in brain are excitotoxic and lead to neuronal death. Glutamate pyrovate transamiase (GPT) and glutamate oxaloacetate transaminase (GOT) catalyze transamination of glutamate to alpha ketoglutarate. Because vitamin B6 is essential for the enzymes activities, this study was undertaken to examine the effect of vitamin B6 on age related changes of this en...

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Difluoro-oxaloacetate interacts with the aldimine form of aspartate transaminase to give a complex, the dissociation constant ofwhich has been determined spectrophotometrically and by 19F n.m.r. (nuclear magnetic resonance). The 19F n.m.r. line-width-pH and chemical-shift-pH profiles of difluoro-oxaloacetate in the presence of the aldimine form of the enzyme both show inflexion points in the pH...

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The intracellular distribution, latency and electrophoretic mobility of L-glutamate-oxaloacetate transaminase from rat liver.

Richardson, E. M., Bulaschenko, H. & Dohan, F. C. (1958). J. clin. Endocrin. 18, 666. Richardson, E. M., Touchstone, J. C., Dohan, F. C., Bulaschenko, H., Landolt, I. & Applin, W. (1955). J. clin. Invest. 34, 285. Rimini, E. (1901). Gazz. chim. ital. 31, II, 84. Romani, J. D. (1956a). C.R. Soc. Biol., Paris, 150, 644. Romani, J. D. (1956b). C.R. Soc. Biol., Paris, 150, 887. Romani, J. D. & Able...

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In a previous publication (1) we have described the synthesis and chemical properties of /3-fluoro-oxaloacetic acid. This acid was found to be a potent inhibitor of mitochondriil malic dehydrogenase (1,2). It is probable that fluoro-oxaloacetate inhibits other enzymes which react with oxaloacetate. We have performed further experiments in order to test this hypothesis. As a part of this study t...

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ژورنال

عنوان ژورنال: Developmental Medicine & Child Neurology

سال: 2017

ISSN: 0012-1622

DOI: 10.1111/dmcn.13310