نتایج جستجو برای: horseradish peroxidase

تعداد نتایج: 30357  

Journal: :Glycobiology 1998
I B Wilson J E Harthill N P Mullin D A Ashford F Altmann

Carbohydrates have been suggested to account for some IgE cross-reactions between various plant, insect, and mollusk extracts, while some IgG antibodies have been successfully raised against plant glycoproteins. A rat monoclonal antibody raised against elderberry abscission tissue (YZ1/2.23) and rabbit polyclonal antiserum against horseradish peroxidase were screened for reactivity in enzyme-li...

Journal: :The Biochemical journal 1985
L Avigliano V Carelli A Casini A Finazzi-Agrò F Liberatore

Horseradish peroxidase catalyses the oxidation of NAD dimers, (NAD)2, to NAD+ in accordance with a reaction that is pH-dependent and requires 1 mol of O2 per 2 mol of (NAD)2. Horseradish peroxidase also catalyses the peroxidation of (NAD)2 to NAD+. In contrast, bacterial NADH peroxidase does not catalyse the peroxidation or the oxidation of (NAD)2. A free-radical mechanism is proposed for both ...

Journal: :iranian journal of chemistry and chemical engineering (ijcce) 2009
iran alemzadeh siamak nejati

horseradish peroxidase was encapsulated in calcium alginate for the purpose of phenol removal. considering enzyme encapsulation efficiency, retention activity and enzyme leakage of the capsules, the best gelation condition was found to be 1 % w/v of sodium alginate solution and 5.5 % w/v of calcium chloride hexahydrate. upon immobilization, ph profile of enzyme activity changes as it shows high...

Journal: :The Journal of biological chemistry 1974
P F Hollenberg T Rand-Meir L P Hager

Chloroperoxidase and horseradish peroxidase use NaClOz as both the oxidant and the halogen donor for the peroxidative chlorination of monochlorodimedone. Previous studies have shown that both horseradish peroxidase and chloroperoxidase can catalyze iodination reactions with hydrogen peroxide as the oxidant; however, only chloroperoxidase catalyzes chlorination reactions under these conditions. ...

Journal: :The Journal of biological chemistry 1977
M Y Wang B M Hoffman P F Hollenberg

Horseradish peroxidase can be reconstituted with cobalt porphyrin to give a cobaltic holoenzyme having physicochemical properties quite similar to those of the native ferric protein. The cobaltic protein (Co3+HRP) can be reduced to the cobaltous form (CoHRP), the analogue of ferroperoxidase and the reduced cobalt protein can bind O2 to form an analogue of oxyferroperoxidase (Compound III). Sinc...

Journal: :Journal of Biological Chemistry 1966

Journal: :biomacromolecular journal 2015
sarah khavari-nejad farnoosh attar

acriflavine (3,6-diaminoacridine) is an anticeptic drug developed in 1912. previous research has focused on investigation of the intercalating features of acriflavine, but little is known about its interaction with proteins. drug-receptor interaction is of major interest in clinical science. the aim of the present study was to evaluate the ability of acriflavine to induce alterations in conform...

2002
BRIAN DUNFORD

The kinetics of the oxidation of p-cresol by Compound II of horseradish peroxidase has been studied by the stopped flow technique at an ionic strength of 0.11 from pH 2 to 11. In acid solution the reaction is kinetically first order in jcresol, but in the alkaline region a saturation effect attributable to complex formation is observed. At very high pH an additional second order reaction betwee...

Journal: :Biochemistry 1996
I E Holzbaur A M English A A Ismail

Fourier transform infrared (FTIR) spectroscopy was employed to examine the thermal denaturation of the Fe(III), Fe(II), and Fe(II)-CO forms of cytochrome c peroxidase and horseradish peroxidase in phosphate buffer at pD 7.0. The amide I' regions of the deconvolved spectra are consistent with predominantly alpha-helical secondary structure around room temperature, but the alpha-helical absorptio...

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