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Size Memory of Casein Colloid Particles

Eastern Utilization Research and Development Division, USDA, Washington, D. C.

ABSTRACT

Fractions of the casein colloid of fresh milk prepared by differential centrifugation, followed by dialysis of each fraction against sodium barbiturate buffer, have been shown by electrophoretic analysis to have the same ratio of - to ß-casein and, by ultra-centrifugal analysis, one major component with a sedimentation (S) value of 5.5 X 10^–13. Other components, present in lower concentrations, appear both in the electrophoretic and in the ultracentrifugal patterns. These sodium caseinate preparations, when re-dialyzed against skimmilk, became opaque and resembled milk. Ultracentrifugal analysis gives S values in the same range as in the original milk. Moreover, the fractions with the larger S values in milk have the larger S values in the reaggregated colloids, ranging from 100 to about 2,000 in the original milk and from 100 to about 400 in the reaggregated colloids.

¹ Present address: W. R. Grace and Co., Washington Research Center, Clarkesville, Maryland.

² Present address: Naval Research Laboratory, Washington, D. C.