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 Pulsed cytochrome c oxidase from the thermophilic bacterium PS3

1984 ◽  
Vol 223 (3) ◽  
pp. 809-813 ◽  
Author(s):  
N Sone ◽  
A Naqui ◽  
C Kumar ◽  
B Chance
Keyword(s):  
Enzyme Activity ◽  
Absorption Spectrum ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Oxidase Activity ◽  
Thermophilic Bacterium ◽  
Decay Process ◽  
Mitochondrial Enzyme ◽  
Bovine Heart ◽  
Enhanced Activity

A caa3-type terminal cytochrome c oxidase (EC 1.9.3.1) from the thermophilic bacterium PS3 containing three subunits showed conversion from resting into pulsed form. Upon pulsing (reduction and re-oxidation), the cytochrome c oxidase activity increased over 10-fold. This enhanced activity of the pulsed enzyme gradually decayed. Addition of phospholipids, necessary for the enzyme activity, did not affect this decay process. Small changes in the absorption spectrum were observed for the resting-into-pulsed transition and for H2O2 ligation to the pulsed enzyme. The e.p.r. spectrum of the resting enzyme was very similar to that of mitochondrial enzyme, but the transient g = 5, 1.78 and 1.69 set of e.p.r. signals, associated with the pulsed bovine heart oxidase, were not observed in the case of pulsed bacterium-PS3 enzyme.

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

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

scholarly journals The interaction of anthraquinone dyes with the plasmid-mediated OXA-2 β-lactamase

1982 ◽  
Vol 205 (2) ◽  
pp. 413-417 ◽  
Author(s):  
C Monaghan ◽  
S Holland ◽  
J W Dale
Keyword(s):  
Specific Effect ◽  
Nucleotide Binding ◽  
Red Shift ◽  
Side Chain ◽  
Beta Lactamase ◽  
Beta Lactamases ◽  
Cibacron Blue ◽  
Anthraquinone Dyes ◽  
Cibacron Blue 3Ga ◽  
Blue Sepharose

Although beta-lactamases do not require any nucleotide co-substrates, the OXA-2 type is inhibited competitively by Cibacron Blue 3GA, and by other anthraquinone dyes, including some simpler compounds with no side chain. The enzyme causes a red shift in the spectrum of Cibacron Blue. The beta-lactamase can be adsorbed in Blue Sepharose and specifically eluted by benzylpenicillin. These results indicate that the binding of anthraquinone dyes is a specific effect similar to that seen with many nucleotide-binding enzymes.

scholarly journals On some properties of catalase haematin

1936 ◽  
Vol 121 (822) ◽  
pp. 173-191 ◽  
Keyword(s):  
Enzyme Activity ◽  
Absorption Spectrum ◽  
High Temperature ◽  
Horse Liver

It was shown recently by Zeile and Hellström (1930) that a strong preparation of catalase obtained from horse liver has the distinct absorption spectrum of a haematin compound. The concentration of this haematin compound in various fractions of their preparations, estimated as pyridine haemochromogen, was found to be proportional to the enzyme activity of these fractions. They have also shown that the factors which abolish or inhibit the activity of the enzyme, such as high temperature, alkali, acids, or the addition of small amounts of KCN or H 2 S, modify also the absorption spectrum of the haematin.

scholarly journals Extruction of keratinase from the local isolate Bacillus licheniformis and partially purified and characterized

2009 ◽  
Vol 3 (2) ◽  
pp. 41-52
Author(s):  
Rasha T. Abdullah ◽  
Abdulkareem J. Hashim ◽  
JASIM M. Karhout
Keyword(s):  
Enzyme Activity ◽  
Bovine Serum Albumin ◽  
Ion Exchange ◽  
Bacillus Licheniformis ◽  
Enzyme Characterization ◽  
Optimal Temperature ◽  
Chicken Feathers ◽  
Local Isolate ◽  
Cellulose Column ◽  
Optimal Ph

The keratinase produced from local isolate Bacillus licheniformis was purified by two steps included precipitation by ammonium sulphate with 40% saturation; followed by ion exchange using CM-Cellulose column. The enzyme was purified to 12.6 times in the last step with an enzyme yield of 17%. Enzyme characterization results indicated that: The optimal pH for enzyme activity was 7.5 and it was stable at 7-9.5. The optimal temperature for enzyme activity was 50°C and it was stable for 30 min at 25-45 °C. Substrate specifity was tested using casein, Bovine serum albumin, gelatin, hooves, human hair, chicken feathers and wool; higher specifity was recorded using casein gave 0.6 unit /ml. The enzyme was inhibited by PMSF and metal ions like Hg+2, Fe+2, Cu+2 and Mn+2, and activated by Ca+2, Mg+2, Zn+2and Al+3.

scholarly journals Comparison of the Affinity Chromatography and the Ion Exchange Chromatography in the Isolation of Bovine Immunoglobin G

OALib ◽  
2014 ◽  
Vol 01 (06) ◽  
pp. 1-5
Author(s):  
Mrigendra Rajput ◽  
Shimaa M. G. Mansour ◽  
Lyle J. Braun ◽  
Mahmoud Darweesh ◽  
Neelu Thakur ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Affinity Chromatography ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Immunoglobin G
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