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[Purine metabolites in the activity of purine nucleoside phosphorylase (author's transl)].
Rev Esp Fisiol. 1976 Sep; 32(3):199-204.RE

Abstract

In the phosphorolytic degradation catalyzed by chicken liver PNPase (E.C. 2.4.2.1) inosine appears to behave as a better substrate than xanthosine. Hypoxanthine, xanthine, guanine and purine (1 X 10(-1)M) appear to be inhibitors of the pigeon liver PNPase, whereas allopurinol, ATP, ITP, CTP and UTP (1. X 10(-3) M) do not inhibit the enzyme. Both PNPase activities exhibit the same optimum temperature (37-40 degrees C). Chicken liver PNPase optimum pH is in the range 6.5-7, whereas that of pigeon liver is in the range 7-7.5. Lineweaver-Burk plots for the inosine phosphorolysis catalyzed by chicken liver PNPase yielded straight lines if substrate concentrations were lower than 1 X 10(-4) M but concave downward curves at higher concentrations. This activation increases when the homogenates are stored at 4 degrees C and pH = 7 during 24 h or more; pigeon liver PNPase does not show this activation phenomenon.

Authors

No affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
English Abstract
Journal Article

Language

spa

PubMed ID

824698

Citation

Fusté, R, and J Bozal. "[Purine Metabolites in the Activity of Purine Nucleoside Phosphorylase (author's Transl)]." Revista Espanola De Fisiologia, vol. 32, no. 3, 1976, pp. 199-204.
Fusté R, Bozal J. [Purine metabolites in the activity of purine nucleoside phosphorylase (author's transl)]. Rev Esp Fisiol. 1976;32(3):199-204.
Fusté, R., & Bozal, J. (1976). [Purine metabolites in the activity of purine nucleoside phosphorylase (author's transl)]. Revista Espanola De Fisiologia, 32(3), 199-204.
Fusté R, Bozal J. [Purine Metabolites in the Activity of Purine Nucleoside Phosphorylase (author's Transl)]. Rev Esp Fisiol. 1976;32(3):199-204. PubMed PMID: 824698.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - [Purine metabolites in the activity of purine nucleoside phosphorylase (author's transl)]. AU - Fusté,R, AU - Bozal,J, PY - 1976/9/1/pubmed PY - 1976/9/1/medline PY - 1976/9/1/entrez SP - 199 EP - 204 JF - Revista espanola de fisiologia JO - Rev Esp Fisiol VL - 32 IS - 3 N2 - In the phosphorolytic degradation catalyzed by chicken liver PNPase (E.C. 2.4.2.1) inosine appears to behave as a better substrate than xanthosine. Hypoxanthine, xanthine, guanine and purine (1 X 10(-1)M) appear to be inhibitors of the pigeon liver PNPase, whereas allopurinol, ATP, ITP, CTP and UTP (1. X 10(-3) M) do not inhibit the enzyme. Both PNPase activities exhibit the same optimum temperature (37-40 degrees C). Chicken liver PNPase optimum pH is in the range 6.5-7, whereas that of pigeon liver is in the range 7-7.5. Lineweaver-Burk plots for the inosine phosphorolysis catalyzed by chicken liver PNPase yielded straight lines if substrate concentrations were lower than 1 X 10(-4) M but concave downward curves at higher concentrations. This activation increases when the homogenates are stored at 4 degrees C and pH = 7 during 24 h or more; pigeon liver PNPase does not show this activation phenomenon. SN - 0034-9402 UR - https://www.unboundmedicine.com/medline/citation/824698/[Purine_metabolites_in_the_activity_of_purine_nucleoside_phosphorylase__author's_transl_]_ DB - PRIME DP - Unbound Medicine ER -
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