Difference between revisions of "Hogeboom 1950 J Biol Chem"
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|abstract=A study is reported of the distribution of isocitric dehydrogenase and | |abstract=A study is reported of the distribution of isocitric dehydrogenase and | ||
TPN-cytochrome c reductase among fractions isolated by differential | TPN-cytochrome c reductase among fractions isolated by differential | ||
centrifugation from homogenates of | centrifugation from homogenates of C3H mouse liver. | ||
Over 80 per cent of the total isocitric dehydrogenase activity of the | Over 80 per cent of the total isocitric dehydrogenase activity of the | ||
homogenates was recovered in a fraction containing the soluble material | 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 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, | Of the total TPN-cytochrome c reductase activity of the homogenates, | ||
over 90 per cent was recovered in the particulate fractions, 49 per cent | 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. | ||
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. | 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. | ||
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|additional=Made history | |additional=Made history | ||
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Revision as of 15:53, 9 June 2012
| 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. |
Hogeboom GH, Schneider WC (1950) 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.
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