Immunological similarity of the cationic and the anionic peanut peroxidase isozymes.
Antibodies against both the native and the deglycosylated cationic peanut peroxidase (C.PRX) were used to probe the structural relationship of this isozyme with its anionic counterpart. Not only the native but also the deglycosylated forms of the cationic and the anionic peroxidases reacted with both antibodies. The activity of the cationic isozymes was inhibited by anti-native C.PRX. Similar but nevertheless distinct immunodetection patterns resulted from reaction of the partially digested cationic and anionic peroxidase peptides with antibodies directed to the deglycosylated as well as to the native C.PRX, suggesting a similarity in their polypeptide structures.
Hu
C F
CF
Department of Plant Sciences, University of Western Ontario London, Canada.
van Huystee
R B
RB
D000838:Anions; D000906:Antibodies / Q000276:immunology; D010367:Arachis / Q000201:enzymology*; D015153:Blotting, Western; D002412:Cations; D003429:Cross Reactions; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes; D006031:Glycosylation; D006868:Hydrolysis; D007527:Isoenzymes / Q000276:immunology*; D010446:Peptide Fragments / Q000032:analysis; D010449:Peptide Mapping; D010544:Peroxidases / Q000037:antagonists & inhibitors / Q000276:immunology*; D011487:Protein Conformation
D000838:Anions; D000906:Antibodies; D002412:Cations; D000939:Epitopes; D007527:Isoenzymes; D010446:Peptide Fragments; D010544:Peroxidases