Results 271 to 280 of about 134,646 (295)
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Transaminases in Neurospora crassa
Nature, 1951THE presence of a wide range of transaminases in both animal tissues1 and bacteria2 has recently been reported. A rather similar array of enzymes appears to be present in the mould Neurospora crassa.
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1979
In summary, several branched-chain fatty acids appeared to be competitive inhibitors of GABA-T and non-competitive inhibitors of SSADH. These compounds produce an increase in brain GABA level, and for two of these it was shown that the increase differs among various brain areas. An increase of GABA cannot be obtained by inhibition of SSADH.
Paul Mandel +8 more
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In summary, several branched-chain fatty acids appeared to be competitive inhibitors of GABA-T and non-competitive inhibitors of SSADH. These compounds produce an increase in brain GABA level, and for two of these it was shown that the increase differs among various brain areas. An increase of GABA cannot be obtained by inhibition of SSADH.
Paul Mandel +8 more
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Experimental Cell Research, 1973
Abstract Aspartic transaminase, tyrosine transaminase, lactic dehydrogenase, and glutamic dehydrogenase were studied in Tetrahymena pyriformis in order to gain a better understanding of the control of the entrance and exit of metabolic intermediates to and from the major carbohydrate pathways.
Pamela Porter, J. Joseph Blum
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Abstract Aspartic transaminase, tyrosine transaminase, lactic dehydrogenase, and glutamic dehydrogenase were studied in Tetrahymena pyriformis in order to gain a better understanding of the control of the entrance and exit of metabolic intermediates to and from the major carbohydrate pathways.
Pamela Porter, J. Joseph Blum
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Serum transaminases in kwashiorkor
The Journal of Pediatrics, 1962Determinations of serum glutamic oxaloacetic and glutamic pyruvic transaminases in children with kwashiorkor failed to show differences between children with “serious” or “early” disease; there was also no change in the concentration of the enzymes after 3 weeks of treatment.
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[15] Glutamate-ornithine transaminases
1985Publisher Summary This chapter provides an overview of glutamate–ornithine transaminases. The simplest assay of δ-ornithine transaminase is based on the formation of a dihydroquinazolinium between Δ 1 -pyrroline-5-carboxylate and o-aminobenzaldehyde. Several radiochemical assays are discussed in the chapter.
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Aminotransferase (Transaminase) Isoenzymes
1970Of the numerous enzymes which reversibly catalyse the transfer of an amino group from an amino acid to an α-keto acid, the two which have been most extensively studied are aspartate aminotransferase (formerly known as glutamate-oxaloacetate transaminase) and alanine aminotransferase (formerly known as glutamate-pyruvate transaminase).
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[11] Glutamate-aspartate transaminase
1985Publisher Summary This chapter focuses on glutamate–aspartate transaminase, an enzyme that is present in microorganisms, plants, and in all animal and human tissues. Its ubiquity attests to its metabolic importance. In addition, in higher organisms, the enzyme exists in soluble (sGOT) and mitochondrial (mGOT) forms.
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MITOCHONDRIAL ASPARTATE TRANSAMINASE
The Lancet, 1970A.M. Nanji, T.R.C. Boyde, S.N. Farmer
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Determination of transaminase.
Methods of biochemical analysis, 2000Alton Meister, Anita J. Aspen
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