Literature DB >> 14195622

A MACROMOLECULAR REPEATING UNIT OF MITOCHONDRIAL STRUCTURE AND FUNCTION. CORRELATED ELECTRON MICROSCOPIC AND BIOCHEMICAL STUDIES OF ISOLATED MITOCHONDRIA AND SUBMITOCHONDRIAL PARTICLES OF BEEF HEART MUSCLE.

H FERNANDEZ MORAN, T ODA, P V BLAIR, D E GREEN.   

Abstract

A repeating particle associated with the cristae and the inner membrane of the external envelope has been recognized and characterized in beef heart mitochondria by correlated electron microscopic and biochemical studies. Many thousands (ca. 10(4) to 10(5)) of these particles, disposed in regular arrays, are present in a single mitochondrion. The repeating particle, called the elementary particle (EP), consists of three parts: (1) a spherical or polyhedral head piece (80 to 100 A in diameter); (2) a cylindrical stalk (about 50 A long and 30 to 40 A wide); and (3) a base piece (40 x 110 A). The base pieces of the elementary particles form an integral part of the outer dense layers of the cristae. The elementary particles can be seen in electron micrographs of mitochondria in situ, of isolated mitochondria, and of submitochondrial particles with a complete electron transfer chain. Negative staining with phosphotungstate is only one of several techniques that can be used for reproducible demonstration of the repeating particles and underlying subunit organization of mitochondrial membranes. A particulate unit containing a complete electron transfer chain can be isolated from beef heart mitochondria. The isolated unit approximates in size that of the elementary particle in situ. The molecular weight of the particle in situ is calculated to be 1.3 x 10(6). Evidence is presented for identifying the isolated unit with the elementary particle visualized in situ. The elementary particle of the mitochondrion is believed to be a prototype of a class of functional particles or macromolecular assemblies of similar size found in association with membranes generally.

Entities:  

Keywords:  BIOCHEMISTRY; CATTLE; COENZYMES; CYTOCHROME OXIDASE; CYTOCHROMES; EXPERIMENTAL LAB STUDY; LIPOPROTEINS; MACROMOLECULAR SYSTEMS; MICROSCOPY, ELECTRON; MITOCHONDRIA; MYOCARDIUM; OXIDOREDUCTASES

Mesh:

Substances:

Year:  1964        PMID: 14195622      PMCID: PMC2106494          DOI: 10.1083/jcb.22.1.63

Source DB:  PubMed          Journal:  J Cell Biol        ISSN: 0021-9525            Impact factor:   10.539


  32 in total

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3.  The macromolecular assembly--a hierarchical entity in cellular organization.

Authors:  F O SCHMITT
Journal:  Dev Biol       Date:  1963-03       Impact factor: 3.582

4.  Studies on the electron transfer system. XLII. Reconstitution of the electron transfer system.

Authors:  Y HATEFI; A G HAAVIK; L R FOWLER; D E GRIFFITHS
Journal:  J Biol Chem       Date:  1962-08       Impact factor: 5.157

5.  Electron Transport in the Oxysome.

Authors:  B Chance; R W Estabrook; C P Lee
Journal:  Science       Date:  1963-04-26       Impact factor: 47.728

6.  Water uptake and extrusion by mitochondria in relation to oxidative phosphorylation.

Authors:  A L LEHNINGER
Journal:  Physiol Rev       Date:  1962-07       Impact factor: 37.312

7.  Cytochemical studies of mitochondria. I. The separation and identification of a membrane fraction from isolated mitochondria.

Authors:  P SIEKEVITZ; M L WATSON
Journal:  J Biophys Biochem Cytol       Date:  1956-11-25

8.  Observations on mitochondrial structure angular configurations of the cristae.

Authors:  J P REVEL; D W FAWCETT; C W PHILPOTT
Journal:  J Cell Biol       Date:  1963-01       Impact factor: 10.539

9.  THE OCCURRENCE OF A SUBUNIT PATTERN IN THE UNIT MEMBRANES OF CLUB ENDINGS IN MAUTHNER CELL SYNAPSES IN GOLDFISH BRAINS.

Authors:  J D ROBERTSON
Journal:  J Cell Biol       Date:  1963-10       Impact factor: 10.539

10.  Electron microscope and low-angle x-ray diffraction studies of the nerve myelin sheath.

Authors:  H FERNANDEZ-MORAN; J B FINEAN
Journal:  J Biophys Biochem Cytol       Date:  1957-09-25
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  51 in total

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Review 2.  LIPIDS OF SUBCELLULAR PARTICLES.

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3.  Cytochemical approaches to the localization of specific adenosine triphosphatases.

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4.  The Heuristic of Form: Mitochondrial Morphology and the Explanation of Oxidative Phosphorylation.

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5.  The ribbon structure of the mitochondrial inner membrane.

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Review 6.  Recent advances in structure-functional studies of mitochondrial factor B.

Authors:  Grigory I Belogrudov
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Review 7.  Structure and function of H+-ATPase.

Authors:  Y Kagawa; N Sone; H Hirata; M Yoshida
Journal:  J Bioenerg Biomembr       Date:  1979-08       Impact factor: 2.945

Review 8.  Once upon a time the cell membranes: 175 years of cell boundary research.

Authors:  Jonathan Lombard
Journal:  Biol Direct       Date:  2014-12-19       Impact factor: 4.540

9.  Contrasting approaches to a biological problem: paul boyer, peter mitchell and the mechanism of the ATP synthase, 1961-1985.

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10.  An ultrastructural study of the hypertrophied human papillary muscle cell with special emphasis on specific staining patterns, mitochondrial projections and association between mitochondria and SR.

Authors:  H Dalen
Journal:  Virchows Arch A Pathol Anat Histopathol       Date:  1989
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