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Guanylate kinases from human erythrocytes, hog brain, and rat liver.
Publisher Summary This chapter describes the purification procedure of guanylate kinases from human erythrocytes, hog brain, and rat liver. A convenient assay involves the measurement of bothExpand
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Tight-binding inhibitors--IV. Inhibition of adenosine deaminases by various inhibitors.
Abstract Three ADA (adenosine deaminase) inhibitors, DHMPR (1,6-dihydro-6-hydroxymethyl purine ribonucleoside); EHNA [erythro-9-(2-hydroxy-3 nonyl)adenine] ; and deoxycoformycin [(R)-3-(2-deoxy-β- dExpand
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Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution.
The three-dimensional structure of human erythrocytic purine nucleoside phosphorylase has been determined at 3.2 A resolution using x-ray diffraction data. Intensity data were measured usingExpand
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[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, whereExpand
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[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 isExpand
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Purine nucleoside phosphorylase from human erythrocytes.
Purine nucleoside phosphorylase has been purified about 7,300-fold and crystallized from human erythrocytes (mol wt 81,000). The recrystallized enzyme exists in the form of needles and sometimesExpand
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  • PDF
Adenosine deaminase from human erythrocytes.
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Adenosine deaminase from human erythrocytes: purification and effects of adenosine analogs.
Abstract Adenosine deaminase (adenosine aminohydrolase, EC 3.5.4.4) has been purified about 3000-fold from human erythrocytes. The molecular weight of the enzyme was estimated to be 33,000. With theExpand
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Tight-binding inhibitors-II. Non-steady state nature of inhibition of milk xanthine oxidase by allopurinol and alloxanthine and of human erythrocytic adenosine deaminase by coformycin.
Abstract The non-steady state nature of the inhibition of milk xanthine oxidase by allopurinol and alloxanthine was demonstrated, and the kinetic data presented are consistent with the knownExpand
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Erythrocytic nucleoside diphosphokinase. II. Isolation and kinetics.
  • N. Mourad, R. Parks
  • Chemistry, Medicine
  • The Journal of biological chemistry
  • 25 January 1966
Abstract Nucleoside diphosphokinase (NDP kinase) was identified in high concentrations in human erythrocytes, and a procedure was developed for the isolation of this enzyme. The best preparations hadExpand
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