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- W2069969881 abstract "Micellar and soluble casein samples were treated with papain which had been cross-linked with glutaraldehyde to form a superpolymer. Unhydrolyzed portions of casein samples were fractionated on polyacrylamide gels. The stained gels were scanned with a densitometer. In both casein samples, the amount of unhydrolyzed κ-, β-, and αs-caseins decreased gradually as the reaction proceeded. The percentage of hydrolysis after 60 min of reaction was 69% in micellar-casein and 78% in soluble casein. However, none of the three casein fractions was hydrolyzed completely. Unhydrolyzed casein in both samples had approximately the same composition throughout the entire reaction. These results suggest that κ-casein does not have a specific location in the casein micelle and that the three major casein fractions are distributed unformly throughout the micelle." @default.
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- W2069969881 date "1971-02-01" @default.
- W2069969881 modified "2023-10-14" @default.
- W2069969881 title "Use of a papain superpolymer to elucidate the structure of bovine casein micelles" @default.
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- W2069969881 doi "https://doi.org/10.1016/0005-2795(71)90201-7" @default.
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