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Purine nucleoside phosphorylase: Isolation and characterization

Collection of Czechoslovak Chemical Communications, 1990
Purine nucleoside phosphorylase (PNP) from mouse leukemia cells L1210 was purified to homogeneity by a combination of ion exchange and affinity chromatography using AE-Sepharose 4B and 9-(p-succinylaminobenzyl)hypoxanthine as the matrix and the ligand, respectively.
Antonín Holý   +3 more
openaire   +2 more sources

Is purine nucleoside phosphorylase an example of a morpheein?

Journal of Physics: Condensed Matter, 2007
Purine nucleoside phosphorylase (PNP) is a ubiquitous enzyme of the nucleoside salvage pathway and it is characterized by non-Michaelis kinetics. Kinetic data in many cases (for some substrates or some concentration range of a co-substrate) are best described by the double hyperbolic equation.
Borys Kierdaszuk   +3 more
openaire   +2 more sources

Computer Simulations Reveal Substrate Specificity of Glycosidic Bond Cleavage in Native and Mutant Human Purine Nucleoside Phosphorylase.

Biochemistry, 2016
Purine nucleoside phosphorylase (PNP) catalyzes the reversible phosphorolysis of purine ribonucleosides and 2'-deoxyribonucleosides, yielding the purine base and (2'-deoxy)ribose 1-phosphate as products.
G. Isaksen   +3 more
semanticscholar   +1 more source

16 Purine Nucleoside Phosphorylase

1972
Publisher Summary This chapter focuses on purine nucleoside phosphorylases (PNPases), which are widely distributed in nature and have been identified and studied in a number of tissues in mammals, chickens, fish, yeast, and in several species of bacteria. In the erythrocytes of dogs, the activity of PNPase is remarkably low when compared with the red
R.E. Parks, R.P. Agarwal
openaire   +2 more sources

Purine nucleoside phosphorylase from bovine liver

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1978
1. Purine nucleoside phosphorylase (purine nucleoside:orthophosphate ribosyltransferase, E.C. 2.4.2.1) from liver of cattle, Bos taurus, was purified to homogeneity. Some properties of the enzymes from three different bovine tissues were compared and discussed. 2.
Takeshi Nishino   +3 more
openaire   +3 more sources

Purine Nucleoside Phosphorylase. 2. Catalytic Mechanism

Biochemistry, 1997
X-ray crystallography, molecular modeling, and site-directed mutagenesis were used to delineate the catalytic mechanism of purine nucleoside phosphorylase (PNP). PNP catalyzes the reversible phosphorolysis of purine nucleosides to the corresponding purine base and ribose 1-phosphate using a substrate-assisted catalytic mechanism.
Richard L. Walter   +4 more
openaire   +3 more sources

A new isotopic assay for purine nucleoside phosphorylase

Analytical Biochemistry, 1989
We have developed a new assay for purine nucleoside phosphorylase which is based on the release of tritium when [2-3H]inosine is used as the substrate and the reaction is coupled with xanthine oxidase. After the reaction is terminated, residual [2-3H]inosine is adsorbed on charcoal and the supernatant solution is assayed for radioactivity by liquid ...
Chi-Hsiung Chang   +2 more
openaire   +3 more sources

Recognition of Artificial Nucleobases by E. coli Purine Nucleoside Phosphorylase versus its Ser90Ala Mutant in the Synthesis of Base-Modified Nucleosides.

Chemistry, 2015
A wide range of natural purine analogues was used as probe to assess the mechanism of recognition by the wild-type (WT) E. coli purine nucleoside phosphorylase (PNP) versus its Ser90Ala mutant.
I. Fateev   +12 more
semanticscholar   +1 more source

Purine Nucleoside Phosphorylase

1985
It has long been appreciated that purine nucleoside phosphorylase (PNP; purine nucleoside: orthophosphate ribosyltransferase, EC 2.4.2.1) may play a role in cancer chemotherapy by catalyzing the degradation of potentially cytotoxic purine deoxynucleoside analogs, e.g., 2′-deoxy-6-thioguanosine.
Johanna D. Stoeckler, Robert E. Parks
openaire   +2 more sources

A new ultramicrochemical assay for purine nucleoside phosphorylase

Analytical Biochemistry, 1978
Abstract An ultramicrochemical method using radioactive substrates has been developed for the quantitation of purine nucleoside phosphorylase (NP) activity in single cells. NP activity can reproducibly be measured in both directions of the enzyme reaction. A quantitative relationship between the number of cells incubated and the NP activity was found.
C. H. M. M. de Bruyn   +4 more
openaire   +3 more sources

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