Hostname: page-component-848d4c4894-2xdlg Total loading time: 0 Render date: 2024-06-17T00:19:04.823Z Has data issue: false hasContentIssue false
  • English
  • Français

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
R. Beeby
Affiliation:
Division of Dairy Research, C.S.I.R.O., Melbourne, Australia
Get access Rights & Permissions [Opens in a new window]

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
Information
Journal of Dairy Research , Volume 32 , Issue 1 , February 1965 , pp. 57 - 63
Copyright
Copyright © Proprietors of Journal of Dairy Research 1965

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Allison, A. C. & Cecil, R. (1958). Biochem. J. 69, 27.CrossRefGoogle Scholar
Beeby, R. (1963). J. Dairy Res. 30, 77.Google Scholar
Beeby, R. (1964). Biochim. biophys. Acta, 82, 418.CrossRefGoogle Scholar
Beeby, R. & Nitschmann, Hs. (1963). J. Dairy Res. 30, 7.CrossRefGoogle Scholar
Brunner, J. R. & Thompson, M. P. (1959). J. Dairy Sci. 42, 1881.CrossRefGoogle Scholar
Hill, R. D. & Hansen, R. R. (1963). J. Dairy Res. 30, 375.CrossRefGoogle Scholar
Jollès, P. & Alais, C. (1960). C.R. Acad. Sci., Paris, 251, 1605.Google Scholar
Jollès, P., Alais, C. & Jollès, J. (1961). Biochim. biophys. Acta, 51, 309.CrossRefGoogle Scholar
Nitschmann, Hs, Wissmann, H. & Henzi, R. (1957). Chimia, 11, 76.Google Scholar
Porath, J. & Flodin, P. (1959). Nature, Lond., 183, 1657.Google Scholar
Sumner, J. B. (1944). Science, 100, 413.CrossRefGoogle Scholar
Warren, L. (1959). J. biol. Chem. 234, 1971.CrossRefGoogle Scholar
Waugh, D. F., Ludwig, Marther, Gillespie, J. M., Garnier, J., Kleiner, Elizabeth S. & Noble, R. W. (1960). Fed. Proc. 19, 337.Google Scholar