Abstract
WHEN rennin is allowed to react with caseins prepared from milk of different ruminant species at neutral pH and in the presence of calcium, paracasein precipitates and the supernatant contains a glycopeptide, called caseino-glycopeptide1: it does not dialyse, and remains soluble in 12 per cent tri-chloroacetic acid (TCA). We prepared and analysed recently the caseino-glycopeptides from cow, goat and sheep caseins, which are analogous but not identical substances1. In the case of cow's casein the glycopeptide was obtained from χ-casein by rennin digestion in the absence of calcium1. χ-casein has been analysed2 and seems to be the specific substrate for rennin. In this paper we want to report the amino-acid composition of human casein and to comment on some results concerning its digestion by rennin.
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ALAIS, C., JOLLÈS, P. Human Casein and its Caseino-glycopeptide. Nature 196, 1098–1099 (1962). https://doi.org/10.1038/1961098a0
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DOI: https://doi.org/10.1038/1961098a0
