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Difference between revisions of "Fernandez-Moran 1962 Circulation"

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{{Publication
{{Publication
|title=Fernandez-Moran H (1962) Cell-membrane ultrastructure. Low-temperature electron microscopy and x-ray diffraction studies of lipoprotein components in lamellar systems. Circulation 26:1039-65.
|title=Fernandez-Moran H (1962) Cell-membrane ultrastructure. Low-temperature electron microscopy and x-ray diffraction studies of lipoprotein components in lamellar systems. Circulation 26:1039-65.
|info=[http://circ.ahajournals.org/content/26/5/1039.full.pdf+html PMID: 13944801 Open Access]
|info=[http://www.ncbi.nlm.nih.gov/pubmed/?term=PMID%3A+13944801 PMID: 13944801]; [http://circ.ahajournals.org/content/26/5/1039.full.pdf+html pdf]
|authors=Fernandez-Moran H
|authors=Fernandez-Moran H
|year=1962
|year=1962
|journal=Circulation
|journal=Circulation
|abstract=The combined electron-microscope and biochemical evidence regarding mitochondria and mitochondrial fractions, although still preliminary in character, indicates that all the functional enzymatic components of the electron-transport chain are compactly arranged in the "elementary particle," which may therefore be regarded as the ultimate unit of mitochondrial function. New data have also been obtained on the hydrated lipoprotein matrix, the recently isolated structural protein, solubilized pure lipid fractions, cytochromes, and other constituent elements of the respiratory-enzyme assemblies.
|abstract=The combined electron-microscope and biochemical evidence regarding mitochondria and mitochondrial fractions, although still preliminary in character, indicates that all the functional enzymatic components of the electron-transport chain are compactly arranged in the "elementary particle," which may therefore be regarded as the ultimate unit of mitochondrial function. New data have also been obtained on the hydrated lipoprotein matrix, the recently isolated structural protein, solubilized pure lipid fractions, cytochromes, and other constituent elements of the respiratory-enzyme assemblies.
|keywords=Mitochondrial structure, electron microscopy, x-ray diffraction
|keywords=Mitochondrial structure, Electron microscopy, X-ray diffraction
}}
}}
{{Labeling
{{Labeling
|additional=Made history
|additional=Made history
}}
}}

Latest revision as of 10:13, 28 May 2015

Publications in the MiPMap
Fernandez-Moran H (1962) Cell-membrane ultrastructure. Low-temperature electron microscopy and x-ray diffraction studies of lipoprotein components in lamellar systems. Circulation 26:1039-65.

Β» PMID: 13944801; pdf

Fernandez-Moran H (1962) Circulation

Abstract: The combined electron-microscope and biochemical evidence regarding mitochondria and mitochondrial fractions, although still preliminary in character, indicates that all the functional enzymatic components of the electron-transport chain are compactly arranged in the "elementary particle," which may therefore be regarded as the ultimate unit of mitochondrial function. New data have also been obtained on the hydrated lipoprotein matrix, the recently isolated structural protein, solubilized pure lipid fractions, cytochromes, and other constituent elements of the respiratory-enzyme assemblies. β€’ Keywords: Mitochondrial structure, Electron microscopy, X-ray diffraction


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Made history