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Apparent Homogeneity of Lactoperoxidase in Gel Electrophoretograms¹

Department of Food Science, Michigan State University, East Lansing

ABSTRACT

Lactoperoxidase (doner: H₂O₂ oxidoreductase, EC 1. 11. 1.7), a heme-containing protein which catalyzes the transfer of oxygen from peroxides to other substances, is one of the principal enzymes found in cows' milk. Polis and Shmukler (4) isolated the enzyme from whey by salt fractionation in alkaline solutions and displacement chromatography on columns of calcium phosphate and silica-calcite. A molecular weight
of 82,000 was reported for the crystallized enzyme. Moving-boundary experiments revealed the presence of two electrophoretically distinct species, designated A and B. Detailed spectral, electrophoretic, and kinetic studies performed on these two enzyme forms caused the authors to conclude that lactoperoxidase A was the native form and form B emanated during isolation. Morrison and Hultquist (2), employing cation exchange resins, obtained the enzyme in a single form in at least four isolations, and two forms were obtained at other times. Groves (1), while working with the red protein encountered lactoperoxidase in his disc electrophoretograms.

¹ Published with the approval of the Michigan Agricultural Experiment Station as Journal Article no. 3892. Supported in part by Graduate Training Grant no. TI ES 16, Division of Environmental Engineering and Food Protection, USPHS.