scholarly journals Biophysical characterization of a recombinant aminopeptidase II from the thermophilic bacterium Bacillus stearothermophilus

2013 ◽  
Vol 40 (1) ◽  
pp. 25-40 ◽  
Author(s):  
Tzu-Fan Wang ◽  
Min-Guan Lin ◽  
Huei-Fen Lo ◽  
Meng-Chun Chi ◽  
Long-Liu Lin
2016 ◽  
Vol 26 (4) ◽  
pp. 730-738 ◽  
Author(s):  
Tingting Yu ◽  
Junmei Ding ◽  
Qingxia Zheng ◽  
Nanyu Han ◽  
Jialin Yu ◽  
...  

PROTEOMICS ◽  
2005 ◽  
Vol 5 (17) ◽  
pp. 4456-4471 ◽  
Author(s):  
Supachai Topanurak ◽  
Supachok Sinchaikul ◽  
Boonyaras Sookkheo ◽  
Suree Phutrakul ◽  
Shui-Tein Chen

2000 ◽  
Vol 10 (4) ◽  
pp. 395-401 ◽  
Author(s):  
Ali Kademi ◽  
Nadra Aı̈t-Abdelkader ◽  
Loubna Fakhreddine ◽  
Jacques C Baratti

1980 ◽  
Vol 191 (2) ◽  
pp. 457-465 ◽  
Author(s):  
I Mains ◽  
D M Power ◽  
E W Thomas ◽  
J A Buswell

An NADH-(dichlorophenol-indophenol) oxidoreductase was purified 104-fold and in 25% overall yield from the thermophilic bacterium Bacillus stearothermophilus, strain PH24. After solubilization in 2M-NaCl at 70 degrees C, the enzyme was purified by ion-exchange and hydroxyapatite chromatography, followed by affinity chromatography on immobilized Cibacron Blue 3GA. The purified enzyme had a mol.wt. of 43 000 and had an absorption spectrum characteristic of flavoprotein. The enzyme activity was enhanced by FMN and by CN-. The enzyme was inhibited by EDTA and by rho-chloromercuribenzoic acid.


1996 ◽  
Vol 178 (19) ◽  
pp. 5586-5591 ◽  
Author(s):  
S A Henstra ◽  
B Tolner ◽  
R H ten Hoeve Duurkens ◽  
W N Konings ◽  
G T Robillard

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