Properties of a non-specific nucleotidase in the membrane of rabbit red cells.
A non-specific nucleotidase was found in rabbit red blood cell membrane and, using 5'-AMP as substrate, several kinetic parameters for the enzyme were determined. Rabbit red cell ghosts catalyzed the hydrolysis of a wide spectrum of nucleoside 5'-, 3'- and 2'-monophosphates and a limited number of non-nucleotide substrates. All these activities were heat inactivated at the same rate, suggesting that they are the result of catalysis by the same enzyme. The nucleotidase was not dependent on K+ or Mg2+ and was also insensitive to ouabain. Its specific activity and other kinetic parameters were identical in preparation of membranes from both reticulocytes and the mature erythrocytes.
D000818:Animals; D002384:Catalysis; D002462:Cell Membrane / Q000201:enzymology; D003854:Deoxyribonucleotides / Q000378:metabolism; D004910:Erythrocyte Membrane / Q000201:enzymology*; D004912:Erythrocytes / Q000201:enzymology*; D006358:Hot Temperature; D007700:Kinetics; D009708:Nucleotidases / Q000378:metabolism*; D011817:Rabbits; D012156:Reticulocytes / Q000201:enzymology; D012265:Ribonucleotides / Q000378:metabolism; D013379:Substrate Specificity
D003854:Deoxyribonucleotides; D012265:Ribonucleotides; D009708:Nucleotidases