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Difference between revisions of "Schneider 1949 J Biol Chem"

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{{Publication
{{Publication
|title=Schneider WC, Potter VR (1949) Intracellular distribution of enzymes; the distribution of oxalacetic oxidase activity in rat liver and rat kidney fractions. J Biol Chem 177: 893-903.  
|title=Schneider WC, Potter VR (1949) Intracellular distribution of enzymes; the distribution of oxalacetic oxidase activity in rat liver and rat kidney fractions. J Biol Chem 177: 893-903.
|info=[http://www.ncbi.nlm.nih.gov/pubmed/18123817 PMID: 18123817]; [http://www.jbc.org/content/177/2/893.full.pdf+html Open Access]
|info=[http://www.ncbi.nlm.nih.gov/pubmed/18123817 PMID: 18123817]; [http://www.jbc.org/content/177/2/893.full.pdf+html Open Access]
|authors=Schneider WC, Potter VR
|authors=Schneider WC, Potter VR
|year=1949
|year=1949
|journal=J Biol Chem
|journal=J Biol Chem
|abstract=# Rat liver and kidney homogenates were fractionated by differential centrifugation into nuclear, mitochondrial, submicroscopic particle, and "soluble" protein fractions and the distribution of nucleic acids and oxalacetic oxidase in these fractions determined.
# The distribution of the nucleic acids in these fractions was to that described in previous work. Desoxypentose nucleic acid was recovered entirely in the nuclear fractions, while pentose nucleic acid (PNA) was found in all the fractions.
# The mitochondrial fractions of these tissues had the highest oxalacetic oxidase activity of the fractions obtained, but this activity accounted for  only about 45 and 30 per cent of the activity of the liver and kidney homogenates respectively. The activity of the other fractions was much lower  that of the mitochondria, and the recovery of oxalacetic oxidase activity in the separate fractions was incomplete but approximately complete recovery was obtained when the enzymatic activities were determined on the recombined fractions.
significance  of  these  findings  was  discussed.  It  was  concluded
that  the  major  portion  of  the  enzymes  of  the  oxalacetic  oxidase  system  is
probably  associated  with  the  mitochondria  of  rat  liver  and  kidney,  but
that  the  full  activity  of  these  enzymes  is  limited  by  the  presence  in
the  other  fractions  of  accessory  enzymes  or  coenzymes.
}}
}}
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{{Labeling
|additional=Made history
|additional=Made history
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Revision as of 18:06, 8 June 2012

Publications in the MiPMap
Schneider WC, Potter VR (1949) Intracellular distribution of enzymes; the distribution of oxalacetic oxidase activity in rat liver and rat kidney fractions. J Biol Chem 177: 893-903.

» PMID: 18123817; Open Access

Schneider WC, Potter VR (1949) J Biol Chem

Abstract:

  1. Rat liver and kidney homogenates were fractionated by differential centrifugation into nuclear, mitochondrial, submicroscopic particle, and "soluble" protein fractions and the distribution of nucleic acids and oxalacetic oxidase in these fractions determined.
  2. The distribution of the nucleic acids in these fractions was to that described in previous work. Desoxypentose nucleic acid was recovered entirely in the nuclear fractions, while pentose nucleic acid (PNA) was found in all the fractions.
  3. The mitochondrial fractions of these tissues had the highest oxalacetic oxidase activity of the fractions obtained, but this activity accounted for only about 45 and 30 per cent of the activity of the liver and kidney homogenates respectively. The activity of the other fractions was much lower that of the mitochondria, and the recovery of oxalacetic oxidase activity in the separate fractions was incomplete but approximately complete recovery was obtained when the enzymatic activities were determined on the recombined fractions.

significance of these findings was discussed. It was concluded that the major portion of the enzymes of the oxalacetic oxidase system is probably associated with the mitochondria of rat liver and kidney, but that the full activity of these enzymes is limited by the presence in the other fractions of accessory enzymes or coenzymes.


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