alpha-Lactalbumin was purified to apparent homogeneity from mouse milk by combined use
of gel filtration, chromatography on DEAE-cellulose and hydroxyapatite, and concanavalin A …

Abstract α-Lactalbumin was purified to homogeneity from rat milk. Rat α-lactalbumin, in
contrast to other α-lactalbumins, is a glycoprotein and exhibits an abnormally high molecular …

Two species of alpha-lactalbumin, alpha-lactalbumin1 and alpha-lactalbumin2, were
separated from rat milk and purified to homogeneity by gel filtration, followed by the DEAE …

Abstract α-Lactalbumin was isolated from the milk of the pig, goat, sheep and human
(American Indian, Negro and Caucasian). Amino acid analyses, spectral properties …

The whey protein, α-lactalbumin, was purified from lactating mammary glands of mice at
high yields. It exists as two major charge forms (pI values of 6.2 and 5.8) with similar …

Abstract α-Lactalbumins isolated from pig, goat, and sheep milk have two electrophoretically
distinct forms as determined by disc gel electrophoresis. Both forms of each species are …

Rat α-lactalbumin, from the milk of Fischer 344 (CDF) rats, was isolated and purified by a
combination of gel filtration and diethylaminoethyl-cellulose ion exchange chromatography …

A simple Chromatographie procedure is presented for isolation of α-lactalbumin from human
whey on columns of DEAE-Sephadex and Sephadex G-100. The protein resembles bovine …

α‐Lactalbumin was isolated from human milk in a yield of 1.8 mg/ml of milk. The purification
procedure involved ammonium sulphate fractionation (30% to 80% saturation) and pH‐4.0 …

Rat alpha-lactalbumin is unique in contrast to alpha-lactalbumin isolated from other species
in that it exists in three charge forms. Each form contains carbohydrate and is active in the …