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Rat alpha-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 electrophoretically distinct proteins had alpha-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 alpha-lactalbumin. Either one or both of two groups of three alpha-lactalbumins were in a given milk sample. The two groups of three alpha-lactalbumins appear to represent two genetic variants upon which is imposed a polymorphic character. All forms of alpha-lactalbumin, within and between strains, were immunologically identical.
R M McKenzie, and
B L Larson
January 1965,
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R M McKenzie, and
B L Larson
March 1968,
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R M McKenzie, and
B L Larson
January 1971,
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R M McKenzie, and
B L Larson
August 1980,
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R M McKenzie, and
B L Larson
April 1975,
Biochemistry,
R M McKenzie, and
B L Larson
October 1976,
Biochemical genetics,
R M McKenzie, and
B L Larson
May 1992,
The Journal of biological chemistry,
R M McKenzie, and
B L Larson
November 1994,
Biochemical Society transactions,
R M McKenzie, and
B L Larson
March 1977,
Biochimica et biophysica acta,
