A New Method for Simultaneous Purification of Cytochrome b5 and NADPH-cytochrome c Reductase from Rat Liver Microsomes

1970 ◽  
Vol 67 (2) ◽  
pp. 249-257 ◽  
Author(s):  
TSUNEO OMURA ◽  
SACHIKO TAKESUE
Keyword(s):  
Cytochrome C ◽  
Rat Liver ◽  
Cytochrome B5 ◽  
Liver Microsomes ◽  
New Method ◽  
Rat Liver Microsomes ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Nadph Cytochrome C Reductase

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.

The binding of NADPH-cytochrome c reductase to rat liver microsomes

1977 ◽  
Vol 77 (3) ◽  
pp. 912-917 ◽  
Author(s):  
Andrey Pokrovsky ◽  
Vladamir Mishin ◽  
Nikolay Rivkind ◽  
Vyacheslav Lyakhovich
Keyword(s):  
Cytochrome C ◽  
Rat Liver ◽  
Liver Microsomes ◽  
Rat Liver Microsomes ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Nadph Cytochrome C Reductase
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