1960, English, Article edition: Tramsamination and the Oxidation of Some Amino-acids by Mung Bean Mitochondria BONE, D. H.; FOWDEN, L.

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Physical Description
  • text/​html
Published
  • Oxford University Press
  • 1960-02-01 00:00:00.0
Language
  • English

Edition details

Title
  • Tramsamination and the Oxidation of Some Amino-acids by Mung Bean Mitochondria
Author
  • BONE, D. H.
  • FOWDEN, L.
Published
  • Oxford University Press
  • 1960-02-01 00:00:00.0
Physical Description
  • text/​html
Subjects
Notes
  • The transaminases for the reaction of α-ketoglutarate with the amino-acids L-alanine, L-aspartic acid, glycine, L-leucine, L-ornithine, and L-valine have been shown to be associated with mung bean mitochondria. Aspartate-glutamate and alanine-glutamate transaminases are two different enzymes both of which are reversible and stimulated by pyridoxal-5′-phosphate. Aspartate is deaminated, with associated oxygen uptake, by mitochondria from 1-day 8eedlings, but there is no oxygen uptake with 2-day mitochondria and aspartate, nor with 1-or 2-day mitochondria and L-alanine, glycine, L-leucine, or L-valine although these amino-acids are all deaminated. The change in aspartate metabolism with increased age of the seedlings is probably due to the reorganization of the enzyme systems which resulted in DPNH being largely oxidized by malic dehydrogenase and oxaloacetate, instead of mainly by a DPNH oxidase.
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  • Copyright (C) 1960, Society for Experimental Biology
Language
  • English
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