• Publications
  • Influence
Guanylate kinases from human erythrocytes, hog brain, and rat liver.
The purified guanylate kinases from the sources that are given in the chapter, were found stable for several years when stored below 0° in the presence of 70% saturated ammonium sulfate.
Tight-binding inhibitors--IV. Inhibition of adenosine deaminases by various inhibitors.
Three ADA (adenosine deaminase) inhibitors, DHMPR, EHNA and deoxycoformycin (a transition state analog), were classified as readily reversible, semi-tight-binding and tight-binding inhibitors.
Purine Nucleoside Phosphorylase
It has long been appreciated that purine nucleoside phosphorylase (PNP; purine nucleoside: orthophosphate ribosyltransferase, EC may play a role in cancer chemotherapy by catalyzing the
Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution.
The specificity of purine nucleoside phosphorylase for guanine, hypoxanthine, and their analogs can be explained on the basis of the arrangement of hydrogen bond donors and acceptors in the active site.
[72] Purine nucleoside phosphorylase from human erythrocytes
Publisher Summary This chapter describes the purification procedure of purine nucleoside phosphorylase (PNPase) enzyme from human erythrocytes. PNPase is crystallized from human erythrocytes, where
[67] Adenosine deaminase from human erythrocytes
Publisher Summary This chapter describes the purification procedure of adenosine deaminase enzyme from human erythrocytes. Among various methods available, the direct spectrophotometric method is
Purine nucleoside phosphorylase from human erythrocytes.
The commercially available bovine spleen purine nucleoside phosphorylase was compared with human erythrocytic enzyme, and in contrast to the behavior of the human enzyme, the spleen enzyme did not display the phenomena of substrate activation at high concentrations of inosine.
Adenosine deaminase from human erythrocytes: purification and effects of adenosine analogs.
Adenosine deaminase (adenosine aminohydrolase, EC 3.5.4) has been purified about 3000-fold from human erythrocytes and Tubercidin (7-deaza- adenosine) and toyocamycin were devoid both of substrate and inhibitor activity.