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Studies on the к-casein complex: II. The isolation of a sialic acid-containing fraction by disrupting the complex at low pH in the presence of sodium chloride

Published online by Cambridge University Press:  01 June 2009

R. Beeby
Affiliation:
Division of Dairy Research, C.S.I.R.O., Melbourne, Australia

Summary

When crude к-casein was precipitated at pH 3 in the presence of 0·4m-NaCl the supernatant contained up to 80% of the total sialic acid but no detectable cystine or cysteine. Two fractions were obtained from this supernatant by chromatography on DEAE cellulose; one containing 4–6% sialic acid and the other only onetenth of this amount.

Most of the sialic acid of the sialic acid-rich fraction was soluble in 12% trichloracetic acid following treatment with rennin. It is suggested that the glycopeptide released by the action of the enzyme on casein originates from this fraction.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1965

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References

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