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Purification of an anionic isoperoxidase from peach seeds and its immunological comparison with other anionic
M A Quesada1, H A Tigier, M J Bukovac
1Dept de Bioquimica y Biologia Molecular, Univ. de Málaga, E-29071 Málaga, Spain; Dept of Horticulture, Michigan State Univ., East Lansing, Ml 48824, USA.
Abstract:
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 mM, 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.

