Peroxidase Isozymes from Horseradish Roots

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Peroxidase Isozymes from Horseradish Roots

Seven peroxidase isozymes were isolated from horseradish roots and purified to homogeneity as ascertained by chromatography, ultracentrifugation, and polyacrylamide disk electrophoresis. Purification procedures included ammonium sulfate precipitation and column chromatography on carboxymethyl and diethylaminoethyl cellulose. Peroxidase activity in the seven isozymes accounted for 86% of the act...

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Peroxidase Isoenzymes from Horseradish Roots

The reactivity of histidine in horseradish peroxidase isoenzymes Al and C was determined by titrating with diazonium-lH-tetrazole. No exposed histidine residue was detected in the native isoenzymes. Upon removal of the heme prosthetic group, however, all three histidine residues became titratable. Studies with p-chloromercuribenzoate and 14C-iodoacetamide indicated that the 6 half-cystine resid...

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Incorporation 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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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...

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Studies 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...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1966

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)96680-9