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  • 1975-1979  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    CEREBRAL AROMATIC AMINOTRANSFERASE (1975)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 25 (1975), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: —Aromatic: 2-oxoglutarate aminotransferase has been purified about 950-fold from rat brain mitochondria. The purified enzyme was homogeneous in polyacrylamide gel electrophoresis and had a molecular weight of approx 63,000. On the basis of substrate specificity, substrate inhibition, purification ratio, yield, polyacrylamide gel electrophoresis and some other properties of the enzyme it has been suggested that brain mitochondrial tyrosine:2-oxoglutarate aminotransferase (l-tyrosine: 2-oxoglutarate aminotransferase, EC 2.6.1.5) is identical with brain mitochondrial phenylalanine and kynurenine: 2-oxoglutarate aminotransferases (l-kynurenine: 2-oxoglutarate aminotransferase, EC 2.6.1.7), and also with aspartate: 2-oxoglutarate aminotransferase (l-aspartate: 2-oxoglutarate aminotransferase, EC 2.6.1.1).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1975.tb04371.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    PURIFICATION, CHARACTERIZATION AND IDENTIFICATION OF TRYPTOPHAN AMINOTRANSFERASE FROM RAT BRAIN (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 27 (1976), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Tryptophan aminotransferase was purified from rat brain extracts. The purified enzyme had an isoelectric point at pH 6.2 and a pH optimum near 8.0. On electrophoresis the enzyme migrated to the anode. The enzyme was active with oxaloacetate or 2-oxoglutarate as amino acceptor but not with pyruvate, and utilized various L-amino acids as amino donors. With 2-oxoglutarate. the order of effectiveness of the L-amino acids was aspartate 〉 5-hydroxytryptophan 〉 tryptophan 〉 tyrosine 〉 phenylalanine. Aminotransferase activity of the enzyme towards tryptophan was inhibited by L-glutamate. Sucrose density gradient centrifugation gave a molecular weight of approx. 55,000. The enzyme was present in both the cytosol and synaptosomal cytosol, but not in the mitochondria. The isoelectrk focusing profile of tryptophan: oxaloacetate aminotransferase activity was identical with that of L-aspartate: 2-oxoglutarate aminotransferase (EC 2.6.1.1) activity, with both subcellular fractions.On the basis of these data, it is suggested that the enzyme is identical with the cytosol aspartate: 2-oxoglutarate aminotransferase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1976.tb00314.x
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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