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Immunoaffinity studies on cationic peanut peroxidase fraction.

Authors :
Chibbar RN
Van Huystee RB
Source :
Journal of plant physiology [J Plant Physiol] 1984; Vol. 116 (4), pp. 365-73. Date of Electronic Publication: 2012 Jan 20.
Publication Year :
1984

Abstract

Cationic peroxidase immobilized on sepharose has been used to separate specific antibodies from the antiperoxidase whole rabbit serum immunoglobulins (IgG) raised against it. The IgGs so separated completely pellet the peroxidase activity of the cationic peroxidase at a ratio of 6 : 1 (w/w). This shows the specificity of purified IgGs which is also shown by the single reaction arc obtained by immunoelectrophoresis of the isolated IgGs followed by challenging with crude peroxidase. These specific IgGs when linked to cyanogen bromide activated sepharose have been used to purify the cationic peroxidase from the spent medium proteins and from the cell extract of the peanut cells grown in suspension culture.<br /> (Copyright © 1984 Gustav Fischer Verlag, Stuttgart. Published by Elsevier GmbH.. All rights reserved.)

Details

Language :
English
ISSN :
0176-1617
Volume :
116
Issue :
4
Database :
MEDLINE
Journal :
Journal of plant physiology
Publication Type :
Academic Journal
Accession number :
23195306
Full Text :
https://doi.org/10.1016/S0176-1617(84)80115-7