The Heterogeneity of Lactoperoxidase.
- 1 January 1965
- journal article
- research article
- Published by Danish Chemical Society in Acta Chemica Scandinavica
- Vol. 19 (10), 2387-2394
- https://doi.org/10.3891/acta.chem.scand.19-2387
Abstract
LactoperoxTdase from cow''s milk was separated into several fractions by chromatography on diethylaminoethyl-Sephadex. The heterogeneity pattern was found to be the same all through the year. All fractions were enzymically active. The main fractions (1 and 2), probably corresponding to lactoperoxidase A and B described by Polis and Schmukler, have the same extinction coefficients at 280 m[mu] but differ in this respect at 412 m[mu]. The iron-content and specific activities, based on the absorption at 280 m[mu], were the same. Lactoperoxidase prepared from a single cow was also heterogeneous.This publication has 4 references indexed in Scilit:
- Lactoperoxidase. IV. Immunological analysis of bovine lactoperoxidase preparations obtained by a simplified fractionation procedureArchives of Biochemistry and Biophysics, 1963
- The Isolation And Purification Of Lactoperoxidase By Ion Exchange ChromatographyJournal of Biological Chemistry, 1957
- Chromatography of Proteins. I. Cellulose Ion-exchange AdsorbentsJournal of the American Chemical Society, 1956
- Stability of Cytochrome c at Extreme pH Values.Acta Chemica Scandinavica, 1948