Electrophoretic analyses revealed protein complexes in milk subjected to different processing. These complexes varied with the type of treatment. Interactions occurred between alpha-and beta-casein; in addition, there was complexing between beta-lactoglobulin and complexed alpha-casein. Milk stored at different temperatures revealed continuous changes. The alphacasein complex was the most labile and dissociated into two major groups, which changed in concentration during storage. Electrophoretie analyses did not reveal the causes of gelation. Editor.
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Fitzpatrick et al. (1957) studied this question.
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