The presence in animal tissues of an enzyme which splits off purines from purine nucleosides has been recognized for many years (1). This enzyme, purine nucleoside phosphorylase (PNP), has been studied by Kalckar (2-4) and has been shown to be involved in the following reaction: ribose-l-purine + phosphate = ribose-1-phosphate + purine Purine nucleoside phosphorylase from rat liver also possesses a certain specificity with regard to the nitrogenous bases. Inosine and guanosine are the only ribosides which undergo phosphorolysis in the presence of the enzyme. Adenosine and xanthosine are inert in the system, as are pyrimidine ribosides. Hypoxanthine and guanine are the only nitrogenous bases which are incorporated into ribosides by the enzyme. Nucleoside phosphorylases fractionated by various means catalyze the phosphorolysis of purine desoxyribosides as well as of the ribosides. Cleavage of the purine base from the pentose does not occur in the ab- (Summer, 1954).It is the purpose of this paper (a) to demonstrate the presence of PNP activity in erythrocytes; (b) to indicate the comparative activity of PNP in the red blood cells of man, dog, rabbit, pig, and chicken; and (c) to report experimentally induced changes in the PNP activity of dog erythrocytes.
METHODSRed cell enzyme preparations were made as follows. Blood obtained by venipuncture was anticoagulated with heparin and centrifuged for 30 minutes at 3,000 r.p.m. The plasma and buffy coat were drawn off. The cells were hemolyzed with distilled water. They were not washed prior to hemolysis since this procedure did not modify the activity of the preparations.