Characterization of plasma membrane redox activity from Ehrlich cells.
Ferricyanide reductase activity of plasma membranes isolated from Ehrlich ascites tumour cells was very sensitive to trypsin treatment. The decreases of activity observed after treatment with different glycosidases suggests that ferricyanide reductase is a glycoprotein. The opposite effects of phospholipase A2 and phospholipase C on the redox activity indicate that the phospholipidic environment plays an important role in the function of ferricyanide reductase. Sodium ions at millimolar concentrations, and some divalent cations at micromolar concentrations (Ca2+, Mg2+, Sr2+, and Mn2+) behaved as stimulators of ferricyanide reductase activity.
Del Castillo-Olivares
A
A
Laboratory of Biochemistry and Molecular Biology, Faculty of Science, University of Málaga, Spain.
Márquez
J
J
Núñez De Castro
I
I
Medina
M A
MA
D000818:Animals; D002286:Carcinoma, Ehrlich Tumor / Q000378:metabolism*; D002413:Cations, Divalent / Q000494:pharmacology; D002462:Cell Membrane / Q000378:metabolism*; D006026:Glycoside Hydrolases / Q000494:pharmacology; D009247:NADH, NADPH Oxidoreductases / Q000187:drug effects / Q000378:metabolism; D010084:Oxidation-Reduction; D010740:Phospholipases / Q000494:pharmacology; D014357:Trypsin / Q000494:pharmacology
D002413:Cations, Divalent; D009247:NADH, NADPH Oxidoreductases; C014227:ferricyanide reductase; D010740:Phospholipases; D006026:Glycoside Hydrolases; D014357:Trypsin