The light side of horseradish peroxidase histochemistry.
نویسندگان
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...
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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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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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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...
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ژورنال
عنوان ژورنال: Journal of Histochemistry & Cytochemistry
سال: 1984
ISSN: 0022-1554,1551-5044
DOI: 10.1177/32.7.6736628