Abstract
1. 1. The removal of the iron from ferrilactin (ferric salt of the bovine whey proteins) has been accomplished by ( a) reduction with SO 2, ( b) reduction with sodium dithionite (Na 2S 2O 4), and ( c) the exchange of Fe +++ with H + by strong cation-exchange resins from an acid solution. 2. 2. A denatured mixture of whey proteins is formed on long contact with a saturated solution of sulfurous acid in the presence of iron salts which is not heat-coagulable at pH 6.7–7.0, and which, although readily digestible in vitro, is of poor biological value unless supplemented with methionine, tryptophan, and arginine. 3. 3. Two protein fractions arise from the dithionite treatment; one is polydisperse electrophoretically and is coagulable by heat. The other has the same ionic mobility at pH 8.6 as β-lactoglobulin and, like β-lactoglobulin, is coagulated by heat at pH 6.7–7.0. 4. 4. Removal of Fe from ferrilactin by ion exchange results in a protein preparation consisting of components having the same ionic mobilities as the principal whey proteins (α-lactalbumin, β-lactoglobulin).
Published Version
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