Delaunay J, Fischer S, Piau J P, Tortolero M, Schapira G
Biochim Biophys Acta. 1978 Dec 8;527(2):425-31. doi: 10.1016/0005-2744(78)90356-x.
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.
