Peroxidase refolding in the presence of specific antibodies

A panel of eight monoclonal antibodies raised against horseradish root peroxidase has been assembled and characterized. Affinity constants were determined for all antibodies, and their specificity for various structural forms of the enzyme (native peroxidase, apoperoxidase, and denatured peroxidase)...

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Bibliographic Details
Published in:	Prikladnaja biohimija i mikrobiologija Vol. 39; no. 5; p. 509
Main Authors:	Bezsudnova, E Iu, Zherdev, A V, Ermolenko, D N, Iakovleva, I V, Sviridov, V V, Popov, V O, Dzantiev, B B
Format:	Journal Article
Language:	Russian
Published:	Russia (Federation) 01-09-2003
Subjects:	Antibodies, Monoclonal - pharmacology Antibody Affinity Antibody Specificity Armoracia - enzymology Benzothiazoles Enzyme Stability Guanidine Peroxidase - immunology Peroxidase - metabolism Plant Roots - enzymology Protein Denaturation Protein Folding Sulfonic Acids - metabolism
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Summary:	A panel of eight monoclonal antibodies raised against horseradish root peroxidase has been assembled and characterized. Affinity constants were determined for all antibodies, and their specificity for various structural forms of the enzyme (native peroxidase, apoperoxidase, and denatured peroxidase) were assessed by competitive enzyme immunoassay. The effects of the antibodies on the process of refolding of peroxidase after its denaturing with 6.5 M guanidine hydrochloride were studied spectrophotometrically, by the restoration of the enzymatic activity in the reaction of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonate). The yield of the active enzyme in the course of the refolding was increased 1.5 to 1.7 times in the presence of antibody H1. Effects of the antibodies constituting the panel on the activity of native peroxidase and the stability of its dilute solutions were analyzed.
ISSN:	0555-1099