scholarly journals STUDIES ON THE FUNCTION OF CELL MEMBRANE 5thREPORT: CHARACTERIZATION OF NADH-CYTOCHROME c REDUCTASE OF LIVER CELL MEMBRANE IN NORMAL AND CCl4-TREATED RATS

1973 ◽  
Vol 23 (5) ◽  
pp. 653-664 ◽  
Author(s):  
Yasusuke MASUDA ◽  
Masato KUCHII ◽  
Hiroyuki YAMAMOTO ◽  
Tadashi MURANO
Keyword(s):  
Cytochrome C ◽  
Cell Membrane ◽  
Liver Cell ◽  
Cytochrome C Reductase ◽  
Liver Cell Membrane ◽  
Nadh Cytochrome

Purification and characterization of a liver cell membrane specific antigen

1986 ◽  
Vol 21 (5) ◽  
pp. 471-478 ◽  
Author(s):  
Shigeru Morichika ◽  
Terukatsu Arima ◽  
Hideo Nagashima
Keyword(s):  
Cell Membrane ◽  
Liver Cell ◽  
Specific Antigen ◽  
Purification And Characterization ◽  
Liver Cell Membrane

Separation and Partial Characterization Of Rat Liver Cell Membrane Components

1971 ◽  
Vol 1 (1) ◽  
pp. 205-220
Author(s):  
Mildred K. Fleetwood ◽  
Roy F. Davis ◽  
Seymour Bakerman
Keyword(s):  
Cell Membrane ◽  
Rat Liver ◽  
Liver Cell ◽  
Partial Characterization ◽  
Liver Cell Membrane ◽  
Membrane Components

scholarly journals Properties of a cytochrome c-enriched light particulate fraction isolated from the photosynthetic bacterium Rhodopseudomonas spheroides

1978 ◽  
Vol 174 (1) ◽  
pp. 267-275 ◽  
Author(s):  
J Barrett ◽  
C N Hunter ◽  
O T G Jones
Keyword(s):  
Cytochrome C ◽  
Sodium Dodecyl ◽  
Photosynthetic Bacterium ◽  
Particulate Fraction ◽  
Cytochrome C Reductase ◽  
Cytochrome C2 ◽  
Succinate Cytochrome C Reductase ◽  
Bulk Membrane ◽  
Nadh Cytochrome ◽  
Rhodopseudomonas Spheroides

Differential centrifugation of suspensions of French-press-disrupted Rhodopseudomonas spheroides yielded a light particulate fraction that was different in many properties from the bulk membrane fraction. It was enriched in cytochrome c and had a low cytochrome b content. When prepared from photosynthetically grown cells this fraction had a very low specific bacteriochlorophyll content. The cytochrome c of the light particles differed in absorption maxima at 77K from cytochrome c2 attached to membranes; there was pronounced splitting of the alpha-band, as is found in cytochrome c2 free in solution. Potentiometric titration at A552–A540 showed the presence of two components that fitted an n = 1 titration; one component had a midpoint redox potential of +345mV, like cytochrome c2 in solution, and the second had E0′ at pH 7.0 of +110 mV, and they were present in a ratio of approx. 2:3. Difference spectroscopy at 77K showed that the spectra of the two components were very similar. More of a CO-binding component was present in particles from photosynthetically grown cells. Light membranes purified by centrifugation on gradients of 5–60% (w/w) sucrose retained the two c cytochromes; they contained no detectable succinate-cytochrome c reductase or bacteriochlorophyll and very little ubiquinone, but they contained NADH-cytochrome c reductase and some phosphate. Electrophoresis on sodium dodecyl sulphate/polyacrylamide gels showed that the light membranes of aerobically and photosynthetically grown cells were very similar and differed greatly from other membrane fractions of R. spheroides.

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