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Eastern Regional Research Laboratory,1 Philadelphia, Pennsylvania
ABSTRACT
The amounts of soluble products resulting from the action of pepsin on whole casein at pH 6.5 have been determined by precipitating the solutions with CaCl2 (clot formation), and with 12% trichloracetic acid, and by adjusting the pH to 4.7 with HCl.
- and ß-Caseins were studied in the same manner; with the latter, however, no clot was obtained. In general, 2 to 5% of the whole casein and
-casein N became soluble by the action of pepsin, with the lower values obtained with trichloracetic acid as the precipitant. Parallel increases in soluble P were obtained. Both paper and column chromatography showed that the soluble fractions contained a number of components, none of which were free amino acids or orthophosphate. Increases in the soluble fraction of ß-casein indicated that considerable proteolysis had occurred. Most of the soluble fractions did not pass through a cellophane membrane.
1 A laboratory of the Eastern Utilization Research and Development Division, Agricultural Research Service, U. S. Department of Agriculture.
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