Properties of vascular ADP-ase.
The properties of vascular ADP-ase were investigated in microsomal preparations of rabbit aortic cell homogenates. The enzyme was found to have a Km of 9 microM. Its activity was not affected by substrates for other purine nucleoside phosphatases nor by substrates for non-specific phosphatases. However, ATP and beta-gamma-methylene ATP inhibited the enzyme. None of sodium fluoride, ouabain, neuraminidase affected ADP-ase activity whereas oligomycin potentiated the activity. The enzyme had an SH requirement and a divalent cation requirement.
D000818:Animals; D001011:Aorta / Q000166:cytology; D001081:Apyrase / Q000097:blood*; D004492:Edetic Acid / Q000494:pharmacology; D008861:Microsomes / Q000201:enzymology; D010744:Phosphoric Monoester Hydrolases / Q000097:blood*; D011817:Rabbits
D004492:Edetic Acid; D010744:Phosphoric Monoester Hydrolases; D001081:Apyrase