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 …

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 …

Homogeneous rat alpha-lactalbumin was prepared from whey by chromatography on DEAE-
Sephadex A-50 and Ultrogel AcA 44. Two biologically active forms of alpha-lactalbumin …

The whey proteins of guinea-pig milk were examined by electrophoresis on paper, cellulose
acetate, starch gel and polyacrylamide gel. 2. Two major proteins were detected, one of …

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 …

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 …

Abstract α-Lactalbumin has been purified from mouse milk by the use of ammonium sulfate
precipitation, Bio-Gel P-100 chromatography and DEAE-cellulose chromatography. Mouse α …

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 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 …

Rajani V. Prasad, Ralph J. Butkowski, James W. Hamilton, and Kurt E. Ebner* abstract: The
amino acid sequence of rat-lactalbumin has been determined. Unlike other-lactalbumins …