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Difference between revisions of "Schnaitman 1967 J Cell Biol"

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(Created page with "{{Publication |title=Schnaitman C, Erwin VG, Greenawalt JW (1967) The submitochondrial localization of monoamine oxidase. An enzymatic marker for the outer membrane of rat liver ...")
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{{Publication
{{Publication
|title=Schnaitman C, Erwin VG, Greenawalt JW (1967) The submitochondrial localization of monoamine oxidase. An enzymatic marker for the outer membrane of rat liver mitochondria. J Cell Biol 32: 719-735. Β 
|title=Schnaitman C, Erwin VG, Greenawalt JW (1967) The submitochondrial localization of monoamine oxidase. An enzymatic marker for the outer membrane of rat liver mitochondria. J Cell Biol 32: 719-735.
|info=[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2107278/pdf/719.pdf PMID: 4291912 Open Access]
|info=[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2107278/pdf/719.pdf PMID: 4291912 Open Access]
|authors=Schnaitman C, Erwin VG, Greenawalt JW
|authors=Schnaitman C, Erwin VG, Greenawalt JW
|year=1967
|year=1967
|journal=J Cell Biol
|journal=J Cell Biol
|abstract=Controlled osmotic lysis (water-washing) of rat liver mitochondria results in a mixed population of small vesicles derived mainly from the outer mitochondrial membrane and of larger bodies containing a few cristae derived from the inner membrane. These elements have been separated on Ficoll and sucrose gradients. The small vesicles were rich in monoamine oxidase, and the large bodies were rich in cytochrome oxidase. Separation of the inner and outer membranes has also been accomplished by treating mitochondria with digitonin in an isotonic medium and fractionating the treated mitochondria by differential centrifugation. Treatment with low digitonin concentrations released monoamine oxidase activity from low speed mitochondrial pellets, and this release of enzymatic activity was correlated with the loss of the outer membrane as seen in the electron microscope. The low speed mitochondrial pellet contained most of the cytochrome oxidase and malate dehydrogenase activities of the intact mitochondria, while the monoamine oxidase activity could be recovered in the form of small vesicles by high speed centrifugation of the low speed supernatant. The results indicate that monoamine oxidase is found only in the outer mitochondrial membrane and that cytochrome oxidase is found only in the inner membrane. Digitonin treatment released more monoamine oxidase than cytochrome oxidase from sonic particles, thus indicating that digitonin preferentially degrades the outer mitochondrial membrane.
|keywords=monoamine oxidase, outer mitochondrial membrane
}}
{{Labeling
|organism=Rat
|tissues=Hepatocyte; Liver
|preparations=Isolated Mitochondria
|enzymes=Marker Enzyme
|additional=Made history
}}
}}
{{Labeling}}

Revision as of 12:26, 20 June 2012

Publications in the MiPMap
Schnaitman C, Erwin VG, Greenawalt JW (1967) The submitochondrial localization of monoamine oxidase. An enzymatic marker for the outer membrane of rat liver mitochondria. J Cell Biol 32: 719-735.

Β» PMID: 4291912 Open Access

Schnaitman C, Erwin VG, Greenawalt JW (1967) J Cell Biol

Abstract: Controlled osmotic lysis (water-washing) of rat liver mitochondria results in a mixed population of small vesicles derived mainly from the outer mitochondrial membrane and of larger bodies containing a few cristae derived from the inner membrane. These elements have been separated on Ficoll and sucrose gradients. The small vesicles were rich in monoamine oxidase, and the large bodies were rich in cytochrome oxidase. Separation of the inner and outer membranes has also been accomplished by treating mitochondria with digitonin in an isotonic medium and fractionating the treated mitochondria by differential centrifugation. Treatment with low digitonin concentrations released monoamine oxidase activity from low speed mitochondrial pellets, and this release of enzymatic activity was correlated with the loss of the outer membrane as seen in the electron microscope. The low speed mitochondrial pellet contained most of the cytochrome oxidase and malate dehydrogenase activities of the intact mitochondria, while the monoamine oxidase activity could be recovered in the form of small vesicles by high speed centrifugation of the low speed supernatant. The results indicate that monoamine oxidase is found only in the outer mitochondrial membrane and that cytochrome oxidase is found only in the inner membrane. Digitonin treatment released more monoamine oxidase than cytochrome oxidase from sonic particles, thus indicating that digitonin preferentially degrades the outer mitochondrial membrane. β€’ Keywords: monoamine oxidase, outer mitochondrial membrane


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Organism: Rat  Tissue;cell: Hepatocyte; Liver"Hepatocyte; Liver" is not in the list (Heart, Skeletal muscle, Nervous system, Liver, Kidney, Lung;gill, Islet cell;pancreas;thymus, Endothelial;epithelial;mesothelial cell, Blood cells, Fat, ...) of allowed values for the "Tissue and cell" property.  Preparation: Isolated Mitochondria"Isolated Mitochondria" is not in the list (Intact organism, Intact organ, Permeabilized cells, Permeabilized tissue, Homogenate, Isolated mitochondria, SMP, Chloroplasts, Enzyme, Oxidase;biochemical oxidation, ...) of allowed values for the "Preparation" property.  Enzyme: Marker Enzyme"Marker Enzyme" is not in the list (Adenine nucleotide translocase, Complex I, Complex II;succinate dehydrogenase, Complex III, Complex IV;cytochrome c oxidase, Complex V;ATP synthase, Inner mt-membrane transporter, Marker enzyme, Supercomplex, TCA cycle and matrix dehydrogenases, ...) of allowed values for the "Enzyme" property. 



Made history