Aspartic-Glutamic Transaminase Activity in Chick Liver

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Glutamic Aspartic Transaminase

Aspartate and glutamate react instantaneously with the pyridoxal form of the pig heart glutamic aspartic transaminase (1) to yield the corresponding keto acid, converting the enzymebound pyridoxal phosphate to bound pyridoxamine phosphate (2). Other amino acids such as methionine sulfoxide, methionine sulfone, and alanine react much more slowly with the enzyme, but the reaction itself appears t...

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Glutamic-aspartic Transaminase. 8. Equilibrium Kinetics with Aspartate.

Pig heart “soluble” glutamic-aspartic transaminase (L-aspartate : 2-oxoglutarate aminotransferase, EC 2.6.1.1) will catalyze the exchange of an amino group between glutamate and ketoglutarate without the participation of any other amino acid or keto acid (1). This “exchange transamination” also occurs between aspartate and oxaloacetate. The rates of these reactions are comparable to the physiol...

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Pig Heart Glutamic Aspartic Transaminase Mechanism of Transamination.

24 Rumberg, B., A. Muller, and H. T. Witt, Nature, 194, 854 (1962). 25 Duysens, L. M. N., and J. Amesz, Biochim. et Biophys. Acta, 64, 261 (1962). 26 Crane, F. L., in CIBA Foundation Symposium on Quinones in Electron Transport (London, 1960), ed. C. E. W. Wolstenholme and C. K. O'Connor (London: J. & A. Churchill, Ltd., 1961), p. 36. 27 Clayton, R. K., Biochem. Biophys. Res. Comm., 9, 49 (1962)...

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Glutamic-glycine Transaminase from Rat Liver.

.ilthough there is ample evidence for the existence of many different transaminases, the lack of progress in the separation of more individually specific transaminases has been lamented by reviewers for a number of years. Transaminations involving glycine or glyoxylate have been studied extensively in crude preparations of animal (1, 2), plants (3), and microorganisms (4), as well as with purif...

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Glutamic aspartic transaminase. II. The influence of pH on absorption spectrum and enzymatic activity.

Isotopes have been used to study transaminases in several ways. Substrates labeled with N15 were used to confirm the fact that transfer occurs between amino acid and keto acid without the formation of ammonia (1, 2), and without any requirement for a specific amino acid such as glutamate (3, 4). Experiments in deuterated water show that the a-hydrogen of the amino acid is liberated as a hydroge...

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ژورنال

عنوان ژورنال: Poultry Science

سال: 1958

ISSN: 0032-5791

DOI: 10.3382/ps.0370096