Immunochemical and immunoelectron microscope studies on localization of NADPH-cytochrome c reductase on rat liver microsomes.
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.
D000818:Animals; D003579:Cytochrome Reductases / Q000032:analysis*; D005455:Fluorescent Antibody Technique; D008297:Male; D008566:Membranes / Q000201:enzymology / Q000648:ultrastructure; D008862:Microsomes, Liver / Q000201:enzymology* / Q000648:ultrastructure; D009251:NADPH-Ferrihemoprotein Reductase / Q000032:analysis*; D051381:Rats
D003579:Cytochrome Reductases; D009251:NADPH-Ferrihemoprotein Reductase