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Purification of an anionic isoperoxidase from peach seeds and its immunological comparison with other anionic isoperoxidases
Author(s) -
Quesada Miguel A.,
Tigier Horacio A.,
Bukovac Martin J.,
Valpuesta Victoriano
Publication year - 1990
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1990.tb00035.x
Subject(s) - polyclonal antibodies , chromatography , size exclusion chromatography , chemistry , sodium dodecyl sulfate , polyacrylamide gel electrophoresis , molecular mass , biochemistry , gel electrophoresis , biology , enzyme , antibody , immunology
A soluble anionic isoperoxidase (EC 1,11,1,7) was purified from peach ( Prunus persica L. Batsch cv. Merry) seeds. Purification was achieved by DEAE‐Sephacel, Sephacryl S‐300 and CM‐cellulose chromatography. The purified isoperoxidase de‐carboxylated indole‐3‐acetic acid (S 0.5 0.13 m M , Hill coefficient 1.7). Molecular mass, determined by gel filtration and sodium dodecyl sulfate polyacrylamide gel electrophoresis, was ca 60 kDa. Polyclonal antibodies were raised in rabbit against this isoperoxidase. Using immunoprecipitation this isoenzyme was found to be immunologically different from other soluble anionic isoperoxidases isolated from peach seeds.