PURIFICATION AND CHARACTERIZATION OF PURINE NUCLEOSIDE PHOSPHORYLASE AND PYRIMIDINE NUCLEOSIDE PHOSPHORYLASE FROM BACILLUS-STEAROTHERMOPHILUS TH-6-2

Authors
HAMAMOTO T NOGUCHI T MIDORIKAWA Y
Citation
T. Hamamoto et al., PURIFICATION AND CHARACTERIZATION OF PURINE NUCLEOSIDE PHOSPHORYLASE AND PYRIMIDINE NUCLEOSIDE PHOSPHORYLASE FROM BACILLUS-STEAROTHERMOPHILUS TH-6-2, Bioscience, biotechnology, and biochemistry, 60(7), 1996, pp. 1179-1180
Citations number
12
Categorie Soggetti
Biology,Agriculture,"Biothechnology & Applied Migrobiology","Food Science & Tenology
Journal title
Bioscience, biotechnology, and biochemistry → ACNP
ISSN journal
09168451
Volume
60
Issue
7
Year of publication
1996
Pages
1179 - 1180
Database
ISI
SICI code
0916-8451(1996)60:7<1179:PACOPN>2.0.ZU;2-B
Abstract
The purine nucleoside phosphorylase (Pu-NPase) and the pyrimidine nucl eoside phosphorylase (Py-NPase) have been purified from Bacillus stear othermophilus 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 Pu-NPase and Py-NPase were pH 4.3 and 4.6, respectively, The Pu-NPase could catalyze the phosphorolysis of inosine and guanosine, but not ad enosine, The Py-NPase could phosphorolyze both uridine and thymidine.