The Effect of Delipidation on the Adenosine Triphosphatase of Sarcoplasmic Reticulum. Electron Microscopy and Physical Properties

1974 ◽  
Vol 42 (1) ◽  
pp. 183-193 ◽  
Author(s):  
N. Michael Green ◽  
Peter M. D. Hardwicke
Keyword(s):  
Electron Microscopy ◽  
Sarcoplasmic Reticulum ◽  
Physical Properties ◽  
Adenosine Triphosphatase

scholarly journals ULTRASTRUCTURE AND ADENOSINE TRIPHOSPHATASE ACTIVITY OF RED AND WHITE MUSCLE FIBERS OF THE CAUDAL REGION OF A FISH, SALMO GAIRDNERI

1972 ◽  
Vol 55 (1) ◽  
pp. 42-57 ◽  
Author(s):  
Asish C. Nag
Keyword(s):  
Electron Microscopy ◽  
Sarcoplasmic Reticulum ◽  
Adenosine Triphosphatase ◽  
White Muscle ◽  
Muscle Fibers ◽  
Salmo Gairdneri ◽  
Fiber Types ◽  
Surface Areas ◽  
Biochemical Studies ◽  
T System

Electron microscopy, together with quantitation using a tracing device linked to a digital computer, reveals that the red and white muscle fibers of Salmo gairdneri differ in diameter, organization of myofibrils, dimensions of myofilaments, volumes and surface areas of T system and sarcoplasmic reticulum, morphology of mitochondria, and content of mitochondria, lipid, and glycogen. Biochemical studies show that the ATPase activity of white fibers is three times that of the red fibers. Actomyosin content of red fibers is higher than that of the white fibers. The functional significance of these differences between two fiber types is discussed.

The Infection of Cells by Bullet-Shaped Viruses

1969 ◽  
Vol 27 ◽  
pp. 372-373
Author(s):  
Frederick A. Murphy ◽  
Alyne K. Harrison ◽  
Sylvia G. Whitfield
Keyword(s):  
Electron Microscopy ◽  
Physical Properties ◽  
Host Cell ◽  
Thin Section ◽  
Cultured Cells ◽  
Cell Infection ◽  
Thin Section Electron Microscopy ◽  
Section Electron ◽  
Section Electron Microscopy

The bullet-shaped viruses are currently classified together on the basis of similarities in virion morphology and physical properties. Biologically and ecologically the member viruses are extremely diverse. In searching for further bases for making comparisons of these agents, the nature of host cell infection, both in vivo and in cultured cells, has been explored by thin-section electron microscopy.

scholarly journals Evidence that coated vesicles isolated from brain are calcium-sequestering organelles resembling sarcoplasmic reticulum.

1977 ◽  
Vol 75 (1) ◽  
pp. 135-147 ◽  
Author(s):  
A L Blitz ◽  
R E Fine ◽  
P A Toselli
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Calcium Ions ◽  
Adenosine Triphosphatase ◽  
Sodium Dodecyl ◽  
Maximal Activity ◽  
Coated Vesicles ◽  
Potassium Oxalate ◽  
Triton X ◽  
Trapping Agent ◽  
The Brain

Coated vesicles from the brain have been purified to near morphological homogeneity by a modification of the method of Pearse. These vesicles resemble sarcoplasmic reticulum fragments isolated from skeletal muscle. They contain proteins with 100,000- and 55,000-dalton mol wt which co-migrate on polyacrylamide gels, in the presence of sodium dodecyl sulfate, with the two major proteins of the sarcoplasmic reticulum fragment. These vesicles contain adenosine triphosphatase (ATPase) activity which is stimulated by calcium ions in the presence of Triton X-100 (Rohm & Haas Co., Philadelphia, Pa.), displaying maximal activity at 8 x 10(-7) M Ca ++. They take up calcium ions from the medium, and this uptake is stimulated by ATP and by potassium oxalate, a calcium-trapping agent. The 100,000-dalton protein of the coated vesicles displays immunological reactivity with an antiserum directed against the 100,000-dalton, calcium-stimulated ATPase of the sarcoplasmic reticulum. As with the sarcoplasmic reticulum fragment, this protein becomes radiolabeled when coated vesicles are briefly incubated with gamma-labeled [32P]ATP. The possible functions of coated vesicles as calcium-sequestering organelles are discussed.

scholarly journals A simple and rapid method for the preparation of adenosine triphosphatase from submitochondrial particles

1975 ◽  
Vol 148 (3) ◽  
pp. 533-537 ◽  
Author(s):  
R B Beechey ◽  
S A Hubbard ◽  
P E Linnett ◽  
A D Mitchell ◽  
E A Munn
Keyword(s):  
Electron Microscopy ◽  
Rapid Method ◽  
Adenosine Triphosphatase ◽  
Pure Form ◽  
Heart Mitochondria ◽  
Polyacrylamide Gels ◽  
Submitochondrial Particles ◽  
Bovine Heart

An almost pure form of the bovine heart mitochondrial adenosine triphosphatase (ATPase) is released from the membrane by shaking submitochondrial particles with chloroform. Analyses on polyacrylamide gels and by electron microscopy, and also sensitivity to inhibitors, show that the chloroform-released enzyme is similar to other ATPase preparations from bovine heart mitochondria.

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