Results 111 to 120 of about 6,269 (168)

Inverse enzyme isotope effects in human purine nucleoside phosphorylase with heavy asparagine labels. [PDF]

open access: yesProc Natl Acad Sci U S A, 2018
Harijan RK   +4 more
europepmc   +1 more source

Study on purine metabolismn Purine nucleoside phosphorylase

open access: yesUric acid research, 1977
Ito, Kazuhiko   +3 more
openaire   +1 more source

Symmetric Nucleosides as Potent Purine Nucleoside Phosphorylase Inhibitors

The Journal of Physical Chemistry B, 2021
Nucleic acids are one of the most enigmatic biomolecules crucial to several biological processes. Nucleic acid-protein interactions are vital for the coordinated and controlled functioning of a cell, leading to the design of several nucleoside/nucleotide analogues capable of mimicking these interactions and hold paramount importance in the field of ...
Pradeep Pant, Amita Pathak, B. Jayaram
openaire   +2 more sources

Purine nucleoside phosphorylase of chicken liver

Biochimica et Biophysica Acta (BBA) - Enzymology, 1971
Abstract Purine nucleoside phosphorylase (purine nucleoside:orthophosphate ribosyltransferase, EC 2.4.2.1) has been purified 125-fold from the homogenate of chicken livers and some of the properties of the purified enzyme have been studied. This enzyme had a pH optimum at around 6.o. At high substrate levels of inosine the reaction rate was increased,
K, Murakami, A, Mitsui, K, Tsushima
openaire   +2 more sources

Characterization of purine nucleoside phosphorylase in leukemia

American Journal of Hematology, 1986
AbstractPurine nucleoside phosphorylase (PNP) activity was determined in mononuclear cells from 49 patients with various types of leukemia. A low level of PNP activity was found in mononuclear cells from patients with acute myeloid and lymphoblastic leukemia and with chronic lymphocytic leukemia. Enzymatic and immunological studies on PNP from leukemic
T, Morisaki   +3 more
openaire   +2 more sources

Adenine as Substrate for Purine Nucleoside Phosphorylase

Canadian Journal of Biochemistry, 1971
Purine nucleoside phosphorylase (purine-nucleoside:orthophosphate ribosyltransferase, EC 2.4.2.1) from four sources (rat liver and brain, human erythrocytes, and calf spleen) has been shown to exhibit a low intrinsic activity towards adenine in the presence of ribose 1-phosphate.
T P, Zimmerman   +3 more
openaire   +2 more sources

Allosteric regulation of purine nucleoside phosphorylase

Archives of Biochemistry and Biophysics, 1991
Purine nucleoside phosphorylase (EC 2.4.2.1) from bovine spleen is allosterically regulated. With the substrate inosine the enzyme displayed complex kinetics: positive cooperativity vs inosine when this substrate was close to physiological concentrations, negative cooperativity at inosine concentrations greater than 60 microM, and substrate inhibition ...
P A, Ropp, T W, Traut
openaire   +2 more sources

Mutations in purine nucleoside phosphorylase deficiency

Human Mutation, 1997
Purine nucleoside phosphorylase deficiency is an inherited disease of purine metabolism characterized clinically as combined immunodeficiency. The molecular defects have been published for 4 different alleles in 3 patients. We report four new mutations including two amino acid substitutions, A174P and G190V, a single codon deletion, delta I129, and a ...
M L, Markert   +8 more
openaire   +2 more sources

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