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Purification and Characterization of Rat -Lactalbumins: Apparent Genetic Variants¹

Department of Dairy Science, University of Illinois, Urbana 61801

ABSTRACT

Rat -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. Three electro-phoretically distinct proteins had -lactalbumin activity. Staining for carbohydrate indicated that at least two of the three forms were glycoproteins. The low molecular weight protein fraction from the wheys of two additional strains of laboratory rat were compared to ascertain whether the composition of this fraction was common in the divergent strains. Outbred Wistar and Long-Evans dams yielded wheys containing up to six forms of -lactalbumin. Either one or both of two groups of three -lactalbumins were in a given milk sample. The two groups of three -lactalbumins appear to represent two genetic variants upon which is imposed a polymorphic character. All forms of -lactalbumin, within and between strains, were immunologically identical.

¹ This investigation was supported under Project US NOl-CB-23856 of the National Cancer Institute, National Institutes of Health, and Hatch Projects 35-320 and 35-351 of the Illinois Agriculture Experiment Station.