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Human Casein and its Caseino-glycopeptide
WHEN rennin is allowed to react with caseins prepared from milk of different ruminant species at neutral p H and in the presence of calcium, paracasein precipitates and the supernatant contains a glycopeptide, called caseino-glycopeptide 1 : it does not dialyse, and remains soluble in 12 per cent tr...
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Published in: | Nature (London) 1962-12, Vol.196 (4859), p.1098-1099 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | WHEN rennin is allowed to react with caseins prepared from milk of different ruminant species at neutral
p
H and in the presence of calcium, paracasein precipitates and the supernatant contains a glycopeptide, called caseino-glycopeptide
1
: 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 substances
1
. In the case of cow's casein the glycopeptide was obtained from χ-casein by rennin digestion in the absence of calcium
1
. χ-casein has been analysed
2
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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ISSN: | 0028-0836 1476-4687 |
DOI: | 10.1038/1961098a0 |