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Summary Coagulation of rennin-treated casein was inhibited by treatment of the casein with dimethylaminonaphthalene sulphonyl chloride. The effect was caused by substitution on lysine side chains of theκ-casein fraction, and inhibition was complete when 2–3 lysine residues/molecule were blocked. This level of substitution did not affect other properties of theκ-casein, such as the release from it of non-protein nitrogen (NPN) by rennin and its ability to stabilizeαs-andβ-caseins in the presence of Ca++. The evidence suggests that lysine side chains onκ-casein take part in the coagulation of rennin-treated casein.
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Hill et al. (1968) studied this question.
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