Difference between revisions of "Hogeboom 1950 J Biol Chem"

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Hogeboom GH, Schneider WC (1950) Cytochemical studies of mammalian tissues III. Isocitric dehydrogenase and triphosphopyridine nucleotide-cytochrome c reductase of mouse liver. J Biol Chem 186: 417-427.

» PMID: 14794638; Open Access

Hogeboom GH, Schneider WC (1950) J Biol Chem

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 {{Publication
 |title=Hogeboom GH, Schneider WC (1950) Cytochemical studies of mammalian tissues III. Isocitric dehydrogenase and triphosphopyridine nucleotide-cytochrome c reductase of mouse liver. J Biol Chem 186: 417-427.
 |info=[http://www.ncbi.nlm.nih.gov/pubmed/14794638 PMID: 14794638]; [http://www.jbc.org/content/186/2/417.full.pdf+html Open Access]
 |authors=Hogeboom GH, Schneider WC
 |year=1950
 |journal=J Biol Chem
-|abstract=A  study  is reported  of  the  distribution  of  isocitric  dehydrogenase  and
-TPN-cytochrome  c  reductase  among  fractions  isolated  by  differential
-centrifugation  from  homogenates  of  C3H mouse  liver.
-Over  80  per  cent  of  the  total  isocitric  dehydrogenase  activity  of  the
-homogenates  was recovered  in  a  fraction  containing  the  soluble  material
-of  the  cytoplasm  of  the  liver  cell.  Of  the  particulate  fractions,  nuclei and  submicroscopic  particles  showed  very  little  activity,  whereas  mitochondria  contained  approximately  12  per  cent  of  the  total.  Results  obtained  with  hypertonic  (0.88  M)  sucrose  as  the  medium  were  essentially  the  same as those  obtained  with  isotonic  (0.25  M)  sucrose.
-Of  the  total  TPN-cytochrome  c reductase  activity  of  the  homogenates,
-over  90  per  cent  was  recovered  in  the  particulate  fractions,  49  per  cent being  present  in  mitochondria  and 36 per  cent  in  submicroscopic  particles. Under  the  conditions  of  the  methods  of  assay,  the  specific  TPN-cytochrome  c reductase  activity  of  mouse  liver  was  found  to  be  much  lower  than  values  previously  reported  for  DPN-cytochrome  c reductase.
-Some  of  the  difficulties  involved  in  the  interpretation  of  data  obtained  with  the  cell  fractionation  technique  are  presented,  and  it  is  concluded  that  several  definite  conditions  must  be  fulfilled  before  a  biochemical  property  can  be  ascribed  to  a  given  structural  component  of  the  cell.
-|keywords=socitric dehydrogenase, triphosphopyridine nucleotide-cytochrome c reductase
 }}
 {{Labeling
-|organism=Mouse
-|tissues=Hepatocyte; Liver
-|preparations=Isolated Mitochondria
-|enzymes=Complex IV; Cytochrome c Oxidase
-|kinetics=Reduced Substrate; Cytochrome c
 |additional=Made history
 }}