TRANSAMINATION WITH PURIFIED ENZYME PREPARATIONS (TRANSAMINASE)

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Transamination with Purified Enzyme Preparations (transaminase)

Braunstein and Kritzmann (1) have reported that with pigeon breast muscle any a-amino acid, with the possible exception of glycine, is active in transamination with either a-ketoglutaric or oxaloacetic acid. On the other hand, the author (2) found that transamination in pigeon breast muscle is limited to the following reactions. a (1) Z(+)-Glutamic acid + oxaloacetic acid e a-ketoglutaric acid ...

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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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Electrophoresis of Purified Antibody Preparations

In connection with a study of the ultracentrifugal sedimentation of antibody preparations (1) the opportunity arose for study of the electrophoretic properties of some of the highly active material under investigation. Measurements of this kind are of value in the characterization of proteins and similar high molecular substances, and may also give information regarding the chemical homogeneity...

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Electrophoresis of Purified Antibody Preparations

In connection with a study of the ultracentrifugal sedimentation of antibody preparations (1) the opportunity arose for study of the electrophoretic properties of some of the highly active material under investigation. Measurements of this kind are of value in the characterization of proteins and similar high molecular substances, and may also give information regarding the chemical homogeneity...

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Electrophoresis of Purified Antibody Preparations

Electrophoretic mobilities of antibody preparations isolated from type specific antipneumococcus horse and rabbit sera, measured over a range of pH values, show that these preparations are distinctly different from normal serum proteins in their electrochemical properties.

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1940

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)73020-2