K Mimori et al.
Annals of oncology : official journal of the European Society for Medical Oncology, 10(1), 111-113 (1999-03-17)
The clinical significance of pyrimidine nucleoside phosphorylase (PyNPase) activity in breast carcinomas has never been determined. In 41 cases of breast carcinoma, the enzyme activity of PyNPase was determined by the high performance liquid chromatography (HPLC) assay and its value...
M J Pugmire et al.
Structure (London, England : 1993), 6(11), 1467-1479 (1998-11-18)
Pyrimidine nucleoside phosphorylase (PYNP) catalyzes the reversible phosphorolysis of pyrimidines in the nucleotide synthesis salvage pathway. In lower organisms (e.g. Bacillus stearothermophilus) PYNP accepts both thymidine and uridine, whereas in mammalian and other higher organisms it is specific for thymidine...
K Okuyama et al.
Bioscience, biotechnology, and biochemistry, 60(10), 1655-1659 (1996-10-01)
The pyrimidine nucleoside phosphorylase (Py-NPase) of Bacillus stearothermophilus TH 6-2 is a dimer of 46-kDa subunits and catalyzes the reversible phosphorolysis of uridine and thymidine. The gene encoding this pyrimidine nucleoside phosphorylase (pyn gene) has been cloned and sequenced from...
T Hamamoto et al.
Bioscience, biotechnology, and biochemistry, 60(7), 1179-1180 (1996-07-01)
The purine nucleoside phosphorylase (Pu-NPase) and the pyrimidine nucleoside phosphorylase (Py-NPase) have been purified from Bacillus stearothermophilus TH 6-2. The Pu-NPase is a trimer of 30-kDa subunits and the Py-NPase is a dimer of 46-kDa subunits. The isoelectric points of...
Purification and comparative properties of a pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus.
P P Saunders et al.
The Journal of biological chemistry, 244(13), 3691-3697 (1969-07-10)