Simultaneous high-performance liquid chromatographic assay of the activities of erythrocytic hypoxanthine-guanine phosphoribosyl transferase and purine nucleoside phosphorylase

1985 ◽  
Vol 349 (2) ◽  
pp. 275-282 ◽  
Author(s):  
Anne P. Halfpenny ◽  
Phyllis R. Brown
Keyword(s):  
High Performance ◽  
Purine Nucleoside Phosphorylase ◽  
High Performance Liquid Chromatographic ◽  
Purine Nucleoside ◽  
Nucleoside Phosphorylase ◽  
Phosphoribosyl Transferase ◽  
Liquid Chromatographic ◽  
Hypoxanthine Guanine Phosphoribosyl Transferase

scholarly journals Elevated erythrocyte phosphoribosylpyrophosphate and ATP concentrations in Japanese sumo wrestlers

1983 ◽  
Vol 49 (1) ◽  
pp. 3-7 ◽  
Author(s):  
Y. Nishida ◽  
I. Akaoka ◽  
E. Hayashi ◽  
T. Miyamoto
Keyword(s):  
Adenosine Deaminase ◽  
Purine Nucleoside Phosphorylase ◽  
Adenine Nucleotides ◽  
Adenosine Kinase ◽  
Purine Nucleoside ◽  
Phosphoribosyl Transferase ◽  
Control Subjects ◽  
Plasma Urate ◽  
And Control ◽  
Hypoxanthine Guanine Phosphoribosyl Transferase

1. Japanese sumo wrestlers have a diet rich in energy, which results in marked obesity. Their plasma urate and triglyceride levels were significantly elevated.2. Erythrocyte phosphoribosylpyrophosphate (PRPP) and ATP concentrations in sumo wrestlers were significantly elevated when compared to the levels in control subjects.3. There were no significant differences in erythrocyte PRPP synthetase (EC 2.7.6.1), purine nucleoside phosphorylase (EC 2.4.2.1) and hypoxanthine guanine phosphoribosyl transferase (EC 2.4.2.8) activities between sumo wrestlers and control subjects.4. Erythrocyte adenosine kinase (EC 2.7.1.20), adenosine deaminase (EC 3.5.4.4) and adenine phosphoribosyl transferase (EC 2.4.2.7) activities in sumo wrestlers were significantly elevated.5. It seems that sumo wrestlers have an increased turnover of adenine nucleotides which may contribute to hyperuricaemia.

scholarly journals Liquid-chromatographic study of purine metabolism abnormalities in purine nucleoside phosphorylase deficiency

1996 ◽  
Vol 42 (2) ◽  
pp. 326-328 ◽  
Author(s):  
C Chantin ◽  
B Bonin ◽  
R Boulieu ◽  
C Bory
Keyword(s):  
Metabolic Disorders ◽  
Purine Nucleoside Phosphorylase ◽  
Purine Nucleoside ◽  
Chromatographic Study ◽  
Guanosine Triphosphate ◽  
Nucleoside Phosphorylase ◽  
Guanosine Diphosphate ◽  
Activity Concentrations ◽  
Purine Nucleoside Phosphorylase Deficiency ◽  
Liquid Chromatographic

Abstract Using HPLC methods, we measured the concentrations of nucleosides and nucleotides for a patient with no purine nucleoside phosphorylase (PNP; EC 2.4.2.1) enzymatic activity. Concentrations of inosine and guanosine were abnormally high in urine and plasma, whereas guanosine diphosphate (GDP) and guanosine triphosphate (GTP) concentrations in erythrocytes were depleted. The unusual presence of deoxyribonucleosides (deoxyinosine and deoxyguanosine) and deoxyribonucleotides (dGDP and dGTP) was also notable. Thus, HPLC represents an accurate and useful tool for the study of purine metabolic disorders.

Stability of Carbovir, a Potent Inhibitor of HIV, to Phosphorolysis by Human Purine Nucleoside Phosphorylase

1992 ◽  
Vol 3 (2) ◽  
pp. 121-124
Author(s):  
C. L. P. Marr ◽  
C. R. Penn
Keyword(s):  
High Pressure ◽  
Hplc Analysis ◽  
Purine Nucleoside Phosphorylase ◽  
Potent Inhibitor ◽  
Antiviral Agent ◽  
Purine Nucleoside ◽  
Nucleoside Phosphorylase ◽  
Hypoxanthine Guanine Phosphoribosyl Transferase ◽  
Hiv 1

Carbovir, a carbocyclic guanosine analogue, is a selective and potent inhibitor of HIV-1 in vitro. The (-)enantiomer of carbovir has been shown, by spectrophotometric and high pressure liquid chromatography (HPLC) analysis, to be stable to phosphorolytic cleavage by purified human erythrocytic purine nucleoside Phosphorylase. Thus depurination, and the salvage reaction via hypoxanthine-guanine phosphoribosyl transferase, would be unlikely to be involved in the metabolism of carbovir. Inhibition of purine nucleoside Phosphorylase interferes with T-lymphocytic function and would be an undesirable activity for any potential antiviral agent. The present study also showed that carbovir, at concentrations up to 300 μM, did not inhibit purine nucleoside Phosphorylase.

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