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Separation and Partial Characterization of the Peroxidases of Ficus glabrata Latex
Author(s) -
KON SAMUEL,
WHITAKER JOHN R.
Publication year - 1965
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1965.tb01873.x
Subject(s) - peroxidase , guaiacol , chemistry , ammonium sulfate precipitation , isoelectric point , chromatography , lactoperoxidase , hydrogen peroxide , isoelectric focusing , biochemistry , size exclusion chromatography , enzyme
SUMMARY Three protein components with peroxidase activity were separated from Ficus glabrata latex by chromatography on diethylaminoethyl cellulose at pH 7.0. Purification was aided by carboxymethyl cellulose adsorption and ammonium sulfate precipitation. These three components were identical to horse‐radish peroxidase II with respect to molecular weights, absorption spectra, and activity‐pH relationships. They differed markedly from horseradish peroxidase II with respect to isoelectric points [at pH 4.25–4.45 (acetate buffer), vs. pH 7.2]. They were more heat‐stable than horse‐radish peroxidase II. While one of the F. glabrata peroxidases had V max values similar to those of horse‐radish peroxidase II on hydrogen peroxide and guaiacol, the other two F. glabrata peroxidases had quite different kinetic parameters. The three F. glabrata peroxidases differed in chromatographic, electrophoretic, heat stability, and kinetic properties (components B and C , vs. A ), but all other properties measured were identical or similar for the three peroxidases.