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 …

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 …

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 …

The antigenic structural features of α-lactalbumin have been investigated using a
radioimmunoassay, peptide inhibition of the quantitative precipitin reaction, and by …

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 …

Rat α-lactalbumin was iódinated by lactoperoxidase, chloramine-T, or monoiodochloride to
a specific activity of 8 µCi/µg, and all retained immunological cross-reactivity. Separation of …

A sensitive and specific radioimmunoassay for human α-lactalbumin, a milk protein, has
been developed in order to examine the effect of prolactin on the human breast in normal …

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 …

Antiserum to purified human α-lactalbumin was produced in rabbits and used to develop a
radioimmunoassay capable of detecting 0.1 ng of α-lactalbumin per ml of sample. Human …

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 …