scholarly journals Effects of Various Compounds on Lipid Peroxidation Mediated by Detergent-Solubilized Rat Liver NADPH-Cytochrome C Reductase

1978 ◽  
Vol 28 (6) ◽  
pp. 837-845 ◽  
Author(s):  
Tetsuya Kamataki ◽  
Osamu Sugita ◽  
Shigeru Naminohira ◽  
Haruo Kitagawa
Keyword(s):  
Lipid Peroxidation ◽  
Cytochrome C ◽  
Rat Liver ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Nadph Cytochrome C Reductase

scholarly journals Electron-transport pathway of the NADH-dependent haem oxygenase system of rat liver microsomal fraction induced by cobalt chloride

1979 ◽  
Vol 178 (2) ◽  
pp. 323-329 ◽  
Author(s):  
Y Hino ◽  
S Minakami
Keyword(s):  
Cytochrome C ◽  
Rat Liver ◽  
Microsomal Fraction ◽  
Cytochrome B5 ◽  
Transport Pathway ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Haem Oxygenase ◽  
Reported Data ◽  
Nadph Cytochrome C Reductase

The hepatic microsomal haem oxygenase activity of rats treated with CoCl2 was studied kinetically by measuring biliverdin, the immediate product of the reaction. Biliverdin was extracted with diethyl ether/ethanol mixture, and was determined by the difference between A690 and A800. The apparent Km value for NADPH (at 50 microM-haematin) was about 0.2 microM when an NADPH-generating system was used, whereas that for NADH was about 630 microM. Essentially the same Vmax. values were obtained for both the NADH- and NADPH-dependent haem oxygenase reactions. No synergism was observed with NADH and NADPH. The NADH-dependent reaction was competitively inhibited by NADP+, with a Ki of about 10 microM. The inhibitoin of the NADH-dependent reaction by the antibody against rat liver microsomal NADPH-cytochrome c reductase was essentially complete, with a pattern similar to that of the NADPH-dependent reaction. The immunochemical experiment and the comparison of the kinetic values with the reported data on isolated NADH-cytochrome b5 reductase and NADPH–cytochrome c reductase indicated the involvement of the latter enzyme in NADH-dependent haem oxygenation by microsomal fraction in situ.

scholarly journals Immunochemical and immunoelectron microscope studies on localization of NADPH-cytochrome c reductase on rat liver microsomes.

1976 ◽  
Vol 68 (2) ◽  
pp. 189-201 ◽  
Author(s):  
T Morimoto ◽  
S Matsuura ◽  
S Sasaki ◽  
Y Yashiro ◽  
T Omura
Keyword(s):  
Cytochrome C ◽  
Rat Liver ◽  
Liver Microsomes ◽  
Morphological Data ◽  
Rat Liver Microsomes ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Antibody Conjugate ◽  
Enzyme Molecules ◽  
Nadph Cytochrome C Reductase

By the use of ferritin-conjugated antibody (conjugate) indirect immunoelectron microscopy, NADPH-cytochrome c reductase was localized on rat liver microsomes. Most microsomes in the sections had from 1 to 12 conjugates on their outer surfaces. Among the conjugates, 83% was estimated to bind to NADPH-cytochrome c reductase at a molecular ratio of 1:1, 12% at the ratio of 2:1, and 5% at the ratio of 3 or 4:1. The correlation between immunochemical and morphological data confirmed that most of the NADPH-cytochrome c reducatase reacted with the conjugates. Subsequent morphological analyses have revealed that the enzyme is distributed homogeneously on the outer surfaces of microsomes but heterogeneously within microsomes in groups of three to five enzyme molecules.

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