R. Parks

Publications171
h-index42
Citations5,723
Highly Influential Citations74
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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 both… Expand
  • 93
  • 8
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- d… Expand
  • 333
  • 4
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 using… Expand
  • 143
  • 4
[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… Expand
  • 104
  • 3
[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… Expand
  • 60
  • 3
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 sometimes… Expand
  • 43
  • 3
  • PDF
Adenosine deaminase from human erythrocytes.
  • 21
  • 3
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 the… Expand
  • 179
  • 2
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 known… Expand
  • 156
  • 2
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 had… Expand
  • 130
  • 2