推薦產品
重組細胞
expressed in E. coli
形狀
liquid
比活性
≥1300 U/mL
相關疾病
cancer
儲存溫度
−20°C
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應用
生化／生理作用
單位定義
One unit will convert 1 μmole each of thymidine and phosphate to thymine and 2-deoxyribose 1-phosphate per minute at pH 7.4 and 25°C
訊號詞
Danger
危險聲明
危險分類
Resp. Sens. 1
儲存類別代碼
12 - Non Combustible Liquids
水污染物質分類（WGK）
WGK 1
閃點（°F）
Not applicable
閃點（°C）
Not applicable
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
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
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
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)
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