Abstract
IT is now known that α-casein from cow milk, which appears electrophoretically homogeneous under many different conditions, consists of at least two compounds which have been designated α- and k-casein1. α-Casein from goat milk, which has similar properties to that from cow milk2 and the same phosphorus content3, showed signs of inhomogeneity during electrophoresis by the moving-boundary method2. Using zone electrophoresis on filter paper it has now been found that the α-component of freshly prepared goat casein does consist of at least two electrophoretically distinct fractions which, until further characterization, will be called α1- and α2-casein in order of decreasing electrophoretic mobility.
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References
Waugh, D., and von Hippel, P. H., J. Amer. Chem. Soc., 78, 4576 (1956).
Dovey, A., and Campbell, P. N., Nature, 169, 1014 (1952).
Hofman, T., Biochem. J. (in the press).
Warner, R. C., J. Amer. Chem. Soc., 66, 1725 (1944).
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HOFMAN, T. Inhomogeneity of α-Casein from Goat Milk. Nature 181, 633–634 (1958). https://doi.org/10.1038/181633b0
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DOI: https://doi.org/10.1038/181633b0
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