title: Purification and characterization of mouse alpha-lactalbumin from lactating mammary glands.
abstract: The whey protein, alpha-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 molecular weights (approx. 14600). Antibodies prepared against these peptides precipitate newly synthesized and secreted alpha-lactalbumin from organ cultures of mid-pregnancy mammary glands. The antibody is specific for mouse alpha-lactalbumin as it does not react with mouse casein, mouse serum or purified bovine alpha-lactalbumin or galactosyl transferase. In addition, it blocks enzymatic activity of alpha-lactalbumin in mouse milk but has no effect on guinea pig or human milk. A very sensitive radioimmunoassay has been developed with this antibody which can detect alpha-lactalbumin levels as low as 0.25 ng.
mesh_terms: D000818:Animals; D005260:Female; D007768:Lactalbumin / Q000096:biosynthesis / Q000302:isolation & purification* / Q000378:metabolism; D007774:Lactation; D008321:Mammary Glands, Animal / Q000502:physiology*; D051379:Mice; D008970:Molecular Weight; D009924:Organ Culture Techniques; D011247:Pregnancy; D011863:Radioimmunoassay
chemical_list: D007768:Lactalbumin