Redox-dependent activation of 5'-nucleotidase in rat liver plasma membranes.
Addition of NADH, but not NAD+ or NADPH, to rat liver plasma membranes resulted in the increase of their 5'-nucleotidase activity. NADH-dependent activation of 5'-nucleotidase was significantly suppressed by atebrine, an inhibitor of NADH dehydrogenase of plasma membranes, and completely abolished by 2,4-dinitrophenol (2 X 10(-4)M) and Triton X-100 (2%). Inhibitors of electron transfer in the mitochondrial respiratory chain, rotenone and potassium cyanide, failed to affect 5'-nucleotidase activity in both the presence and absence of NADH. The data obtained give reasons to suggest a redox-dependent mechanism of 5'-nucleotidase activation in rat liver plasma membranes.
D019297:2,4-Dinitrophenol; D015720:5'-Nucleotidase; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D004140:Dinitrophenols / Q000494:pharmacology; D004789:Enzyme Activation; D008099:Liver / Q000201:enzymology*; D008297:Male; D009243:NAD / Q000378:metabolism; D009245:NADH Dehydrogenase / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D009708:Nucleotidases / Q000378:metabolism*; D017830:Octoxynol; D010084:Oxidation-Reduction; D011092:Polyethylene Glycols / Q000494:pharmacology; D051381:Rats
D004140:Dinitrophenols; D009243:NAD; D011092:Polyethylene Glycols; D009249:NADP; D017830:Octoxynol; D009245:NADH Dehydrogenase; D009708:Nucleotidases; D015720:5'-Nucleotidase; D019297:2,4-Dinitrophenol