scholarly journals Functional proteomics and correlated signaling pathway of the thermophilic bacterium Bacillus stearothermophilus TLS33 under cold-shock stress

PROTEOMICS ◽  
2005 ◽  
Vol 5 (17) ◽  
pp. 4456-4471 ◽  
Author(s):  
Supachai Topanurak ◽  
Supachok Sinchaikul ◽  
Boonyaras Sookkheo ◽  
Suree Phutrakul ◽  
Shui-Tein Chen
Keyword(s):  
Signaling Pathway ◽  
Bacillus Stearothermophilus ◽  
Cold Shock ◽  
Thermophilic Bacterium ◽  
Functional Proteomics ◽  
Bacterium Bacillus ◽  
Shock Stress

Proteomics of early and late cold shock stress on thermophilic bacterium, Thermus sp. GH5

2011 ◽  
Vol 74 (10) ◽  
pp. 2100-2111 ◽  
Author(s):  
Masoumeh Yousefi-Nejad ◽  
Hossein Naderi- Manesh ◽  
Khosro Khajeh
Keyword(s):  
Cold Shock ◽  
Thermophilic Bacterium ◽  
Shock Stress

Investigation of oxidative condition after cold shock stress on thermophilic bacterium, Thermus sp. GH5

2011 ◽  
Vol 44 (13) ◽  
pp. S32-S33
Author(s):  
Masomeh Yousefi-Nejad ◽  
Hossein Naderi-Manesh ◽  
Khosro Khajeh
Keyword(s):  
Cold Shock ◽  
Thermophilic Bacterium ◽  
Oxidative Condition ◽  
Shock Stress

scholarly journals Purification of an NADH-(dichlorophenol-indophenol) oxidoreductase from Bacillus stearothermophilus

1980 ◽  
Vol 191 (2) ◽  
pp. 457-465 ◽  
Author(s):  
I Mains ◽  
D M Power ◽  
E W Thomas ◽  
J A Buswell
Keyword(s):  
Enzyme Activity ◽  
Absorption Spectrum ◽  
Ion Exchange ◽  
Affinity Chromatography ◽  
Bacillus Stearothermophilus ◽  
Thermophilic Bacterium ◽  
Cibacron Blue ◽  
Cibacron Blue 3Ga ◽  
Spectrum Characteristic ◽  
Bacterium Bacillus

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.

scholarly journals Cloning, expression, and isolation of the mannitol transport protein from the thermophilic bacterium Bacillus stearothermophilus.

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
Keyword(s):  
Bacillus Stearothermophilus ◽  
Thermophilic Bacterium ◽  
Transport Protein ◽  
Bacterium Bacillus

Identification and Characterization of a New Alkaline SGNH Hydrolase from a Thermophilic Bacterium Bacillus sp. K91

2016 ◽  
Vol 26 (4) ◽  
pp. 730-738 ◽  
Author(s):  
Tingting Yu ◽  
Junmei Ding ◽  
Qingxia Zheng ◽  
Nanyu Han ◽  
Jialin Yu ◽  
...  
Keyword(s):  
Thermophilic Bacterium ◽  
Bacillus Sp ◽  
Bacterium Bacillus ◽  
Identification And Characterization
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