ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
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 Vmax 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1965.tb01873.x
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