Purification of rat-liver γ-hydroxyglutamate transminase and its probable identity with glutamate-aspartate transminase
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چکیده
منابع مشابه
Mouse liver epoxide hydratase: purification and identity with the rat liver enzyme [proceedings].
Barry, S. & O'Carra, P. (1973) Biochem. J. 135,595-607 Bohme, H. J., Kopperschlager, G., Schulz, J. & Hofman, E. (1972) J. Chrornatogr. 69,209-214 Cuatrecasas, P. (1970) J. Biol. Chem. 245, 3059-3065 Easterday, R. L. & Easterday, I. M. (1974) Adu. Exp. Med. Biol. 42, 123-133 Eventhoff, W. & Rossman, M. G. (1976) Trends Biochem. Sci. 1, 227-230 Jervis, L. (1977) Chromatographic Fractionation of ...
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Kinetics and regulation of the glutamate-aspartate translocator in rat liver mitochondria.
The kinetics and mechanism of the electrogenic exchange of external glutamate with intramitochondrial aspartate have been investigated using aspartateloaded rat liver mitochondria in the absence of metabolism. Apparent kinetic constants were calculated from measured decreases of the mitochondrial matrix aspartate content after glutamate addition by a computer curve fitting procedure and by grap...
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1. Aspartate-carbamoyltransferase activity was concentrated from rat-liver preparations. Only l-aspartate, beta-benzyl-l-aspartate and beta-erythro-hydroxy-dl-aspartate were carbamoylated enzymically. The K(m) for l-aspartate and carbamoyl phosphate have been determined by three methods: colorimetric procedure, radioactive assay with [(14)C]aspartate and an assay with [(14)C]carbamoyl phosphate...
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Glutamate dehydrogenase has been purified and crystallized from rat liver mitochondria and from whole rat liver preparations. No differences in the enzyme prepared by the two different methods have been observed and there is no evidence that more than one glutamate dehydrogenase occurs in rat liver. The pure enzyme has a molecular weight of 350,000 f 20,000 and consists of six to eight subunits...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects
سال: 1964
ISSN: 0926-6569
DOI: 10.1016/0926-6569(64)90136-1