The structure of a neural specific carbohydrate epitope of horseradish peroxidase recognized by anti-horseradish peroxidase antiserum
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چکیده
منابع مشابه
Cobalt-substituted horseradish peroxidase.
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...
متن کاملStudies on Horseradish Peroxidase
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...
متن کاملOxidation of NAD dimers by horseradish peroxidase.
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 ...
متن کاملMechanism of Oxidation by Horseradish Peroxidase Compound
Binding of p-cresol to native horseradish peroxidase was investigated by differential spectrophotometry, and the value lo3 Kdiss = 3 M was obtained at neutral and acid pH; binding is not competitive with that of cyanide and hydroxide. The Soret region spectrum of Compound II of the enzyme was measured in the steady state at pH 4.26, 6.89, and 10.95, and the differences were found to be too smal...
متن کاملIncorporation of carbohydrate residues into peroxidase isoenzymes in horseradish roots.
Sliced root tissue of the horseradish plant (Armoracia rusticana), when incubated with mannose-U-(14)C, incorporated radioactivity into peroxidase isoenzymes. Over 90% of the radioactivity in the highly purified peroxidase isoenzymes was present in the neutral sugar residues of the molecule, i.e. fucose, arabinose, xylose, mannose. When the root slices were incubated simultaneously with leucine...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1991
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(20)64302-2