Guanidine Hydrochloride Induced Equilibrium Unfolding Studies of Colicin B and Its Channel-Forming Fragment

Biochemistry ◽  
2002 ◽  
Vol 41 (17) ◽  
pp. 5340-5347 ◽  
Author(s):  
H. A. Sathish ◽  
Monica Cusan ◽  
Christopher Aisenbrey ◽  
Burkhard Bechinger
Keyword(s):  
Guanidine Hydrochloride ◽  
Equilibrium Unfolding ◽  
Colicin B

Equilibrium unfolding of DLC8 monomer by urea and guanidine hydrochloride: Distinctive global and residue level features

Biochimie ◽  
2007 ◽  
Vol 89 (1) ◽  
pp. 117-134 ◽  
Author(s):  
Amarnath Chatterjee ◽  
P.M. Krishna Mohan ◽  
Arati Prabhu ◽  
Anindya Ghosh-Roy ◽  
Ramakrishna V. Hosur
Keyword(s):  
Guanidine Hydrochloride ◽  
Residue Level ◽  
Equilibrium Unfolding

scholarly journals Folding mechanism of canine milk lysozyme studied by circular dichroism and fluorescence spectroscopy

2003 ◽  
Vol 17 (2-3) ◽  
pp. 183-193 ◽  
Author(s):  
Masaharu Nakao ◽  
Munehito Arai ◽  
Takumi Koshiba ◽  
Katsutoshi Nitta ◽  
Kunihiro Kuwajima
Keyword(s):  
Circular Dichroism ◽  
Fluorescence Spectroscopy ◽  
Molten Globule ◽  
Guanidine Hydrochloride ◽  
Folding Intermediates ◽  
Equilibrium Unfolding ◽  
Burst Phase ◽  
The Relationship ◽  
Kinetics Of ◽  
Circular Dichroïsm

We have studied the guanidine hydrochloride‒induced equilibrium unfolding and the kinetics of refolding of canine milk lysozyme by circular dichroism and fluorescence spectroscopy. The thermodynamic analysis of the equilibrium unfolding measured by circular dichroism and fluorescence has shown that unfolding is represented by a three‒state mechanism and that the intermediate state of canine milk lysozyme is remarkably more stable than the intermediates observed in other lysozyme and α-lactalbumin. In the kinetic refolding of this protein, there are at least two kinetic intermediates; a burst=phase intermediate accumulated within the dead time (4 ms) of the measurement and an intermediate that has been observed during the kinetics with a rate constant of 10–20 s–1after the burst phase. This result is apparently in contrast with those previously observed in the kinetic refolding of α‒lactalbumin and equine lysozyme that show only the burst‒phase intermediate. The relationship between the extraordinarily stable equilibrium molten globule and the kinetic folding intermediates will be discussed.

On the Preparation of Bovine α-Thrombin

1978 ◽  
Vol 39 (01) ◽  
pp. 193-200 ◽  
Author(s):  
Erwin F Workman ◽  
Roger L Lundblad
Keyword(s):  
Immobilized Enzyme ◽  
Catalytic Properties ◽  
Specific Activity ◽  
Guanidine Hydrochloride ◽  
Low Molecular Weight ◽  
Reversible Process ◽  
Gel Beads ◽  
Tissue Thromboplastin ◽  
C 50 ◽  
Hydrolysis Of

SummaryAn improved method for the preparation of bovine α-thrombin is described. The procedure involves the activation of partially purified prothrombin with tissue thromboplastin followed by chromatography on Sulfopropyl-Sephadex C-50. The purified enzyme is homogeneous on polyacrylamide discontinuous gel electrophoresis and has a specific activity toward fibrinogen of 2,200–2,700 N.I.H. U/mg. Its stability on storage in liquid media is dependent on both ionic strenght and temperature. Increasing ionic strength and decreasing temperature result in optimal stability. The denaturation of α-thrombin by guanidine hydrochloride was found to be a partially reversible process with the renatured species possessing properties similar to “aged” thrombin. In addition, the catalytic properties of a-thrombin covalently attached to agarose gel beads were also examined. The activity of the immobilized enzyme toward fibrinogen was affected to a much greater extent than was the hydrolysis of low molecular weight, synthetic substrates.

Influence of mixed aqueous solutions of polyhexamethylene guanidine hydrochloride and OP-10 on vegetable crop seeds

2018 ◽  
Vol 11 (2) ◽  
pp. 164-172
Author(s):  
О.A. Yessimova ◽  
◽  
А.О. Adilbekova ◽  
M.Zh. Kerimkulova ◽  
G.D. Isenova ◽  
...  
Keyword(s):  
Aqueous Solutions ◽  
Guanidine Hydrochloride ◽  
Vegetable Crop ◽  
Polyhexamethylene Guanidine

Green Formation of Novel Pyridinyltriazole-Salicylidene Schiff Bases

2019 ◽  
Vol 16 (2) ◽  
pp. 309-313
Author(s):  
Mustafa Kemal Gümüş
Keyword(s):  
Microwave Irradiation ◽  
Schiff Bases ◽  
Guanidine Hydrochloride ◽  
Alternative Methods ◽  
Second Step ◽  
Green Method ◽  
Maximum Reaction ◽  
Pyridine Carboxylic ◽  
High Yields ◽  
Amine Hydrochlorides

Aim and Objective: In this work, water was used as solvent for the eco-friendly synthesis of imines under microwave irradiation. In the first step of the study, 5-pyridinyl-3-amino-1,2,4-triazole hydrochlorides were synthesized in the reaction of amino guanidine hydrochloride with different pyridine carboxylic acids under acid catalysis. A green method for 5-pyridinyl-3-amino-1,2,4-triazoles was developed with the assistance of microwave synthesis. In the second step, the eco-friendly synthesis of imines was achieved by reacting 5- pyridinyl-2H-1,2,4-triazol-3-amine hydrochlorides with salicylic aldehyde derivatives to produce 2-(5- pyridinyl-2H-1,2,4-triazol-3-ylimino)methyl)phenol imines. Materials and Methods: Microwave experiments were done using a monomode Anton Paar Monowave 300 microwave reactor (2.45 GHz). Reaction temperatures were monitored by an IR sensor. Microwave experiments were carried out in sealed microwave process vials G10 with maximum reaction volume of 10 mL. Results: When alternative methods were used, it was impossible to obtain good yields from ethanol. Nevertheless, the use of water was successful for this reaction. After 1-h microwave irritation, a yellow solid was obtained in 82% yield. Conclusion: In this work an eco-friendly protocol for the synthesis of Schiff bases from 5-(pyridin-2-, 3- or 4- yl)-3-amino-1,2,4-triazoles and substituted salicylic aldehydes in water under microwave irradiation was developed. Under the found conditions the high yields for the products were achieved at short reaction time and with an easy isolation procedure.

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