Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1973 Dec;135(4):875–880. doi: 10.1042/bj1350875

Isolation and characterization of a glycoprotein from human colostrum*

James H Nichols 1, Anatoly Bezkorovainy 1
PMCID: PMC1165907  PMID: 4778282

Abstract

A glycoprotein was isolated from the M-1 acid glycoprotein fraction of human colostrum. It had a molecular weight of 31200 and contained 27% galactose, 21.7% hexosamine, 8.0% fucose and 10.8% sialic acid by weight. The glycoprotein had no absorption maxima in the 240–300nm region, and was virtually free of ABH(O) and M and N blood-group activity. Alkaline borohydride cleavage of the glycoprotein resulted predominantly in the destruction of threonine and galactosamine.

Full text

PDF
875

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. ADAMS J. B. STUDIES ON THE MUCIN DERIVED FROM HUMAN COLLOID BREAST CARCINOMA. Biochem J. 1965 Feb;94:368–377. doi: 10.1042/bj0940368. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. ANDERSON B., HOFFMAN P., MEYER K. THE O-SERINE LINKAGE IN PEPTIDES OF CHONDROITIN 4- OR 6-SULFATE. J Biol Chem. 1965 Jan;240:156–167. [PubMed] [Google Scholar]
  3. Allen W. S., Wardi A. H. Pentose-rich glycoprotein from bovine vitreous body. I. Isolation and partial characterization. Biochim Biophys Acta. 1973 Jan 24;297(1):1–10. doi: 10.1016/0304-4165(73)90043-3. [DOI] [PubMed] [Google Scholar]
  4. Bezkorovainy A. Comparative study of the acid glycoproteins isolated from bovine serum, colostrum, and milk whey. Arch Biochem Biophys. 1965 Jun;110(3):558–567. doi: 10.1016/0003-9861(65)90450-9. [DOI] [PubMed] [Google Scholar]
  5. Bezkorovainy A., Grohlich D. Separation of the bovine colostrum M-1 glycoprotein into two components. Biochem J. 1969 Dec;115(4):817–822. doi: 10.1042/bj1150817. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Bezkorovainy A. Physical and chemical properties of bovine milk and colostrum whey M-1 glycoproteins. J Dairy Sci. 1967 Sep;50(9):1368–1375. doi: 10.3168/jds.S0022-0302(67)87637-9. [DOI] [PubMed] [Google Scholar]
  7. Bezkorovainy A. Ultracentrifugal behavior of transferrin in the presence of some anions. Biochim Biophys Acta. 1966 Oct 10;126(2):286–291. doi: 10.1016/0926-6585(66)90065-3. [DOI] [PubMed] [Google Scholar]
  8. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  9. Donald A. S., Creeth J. M., Morgan W. T., Watkins W. M. The peptide moiety of human-blood-group active glycoproteins associated with the ABO and Lewis groups. Biochem J. 1969 Oct;115(1):125–127. doi: 10.1042/bj1150125. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. GOT R., FONT J., BOURRILLON R., CORNILLOT P. [Human colostrum. Chromatography on DEAE-cellulose of the glycopeptide fraction soluble in 50 per cent ethanol]. Biochim Biophys Acta. 1963 Jul 16;74:247–254. doi: 10.1016/0006-3002(63)91363-5. [DOI] [PubMed] [Google Scholar]
  11. GYORGY P., KUHN R., ROSE C. S., ZILLIKEN F. Bifidus factor. II. Its occurrence in milk from different species and in other natural products. Arch Biochem Biophys. 1954 Jan;48(1):202–208. doi: 10.1016/0003-9861(54)90324-0. [DOI] [PubMed] [Google Scholar]
  12. GYORGY P., NORRIS R. F., ROSE C. S. Bifidus factor. I. A variant of Lactobacillus bifidus requiring a special growth factor. Arch Biochem Biophys. 1954 Jan;48(1):193–201. doi: 10.1016/0003-9861(54)90323-9. [DOI] [PubMed] [Google Scholar]
  13. Gatt R., Berman E. R. A rapid procedure for the estimation of amino sugars on a micro scale. Anal Biochem. 1966 Apr;15(1):167–171. doi: 10.1016/0003-2697(66)90262-4. [DOI] [PubMed] [Google Scholar]
  14. Hirano S., Hayashi H., Terabayashi T., Onodera K., Iseki S. Biologically active glycopeptides in human colostrum. J Biochem. 1968 Oct;64(4):563–565. doi: 10.1093/oxfordjournals.jbchem.a128931. [DOI] [PubMed] [Google Scholar]
  15. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  16. McGuire E. J., Roseman S. Enzymatic synthesis of the protein-hexosamine linkage in sheep submaxillary mucin. J Biol Chem. 1967 Aug 25;242(16):3745–3747. [PubMed] [Google Scholar]
  17. REISSIG J. L., STORMINGER J. L., LELOIR L. F. A modified colorimetric method for the estimation of N-acetylamino sugars. J Biol Chem. 1955 Dec;217(2):959–966. [PubMed] [Google Scholar]
  18. SPRINGER G. F. Inhibition of blood-group agglutinins by substances occurring in plants. J Immunol. 1956 Jun;76(6):399–407. [PubMed] [Google Scholar]
  19. Springer G. F., Nagai Y., Tegtmeyer H. Isolation and properties of human blood-group NN and meconium-Vg antigens. Biochemistry. 1966 Oct;5(10):3254–3272. doi: 10.1021/bi00874a028. [DOI] [PubMed] [Google Scholar]
  20. WARREN L. The thiobarbituric acid assay of sialic acids. J Biol Chem. 1959 Aug;234(8):1971–1975. [PubMed] [Google Scholar]
  21. Weber P., Winzler R. J. Determination of hexosaminitols by ion-exchange chromatography and its application to alkali-labile glycosidic linkages in glycoproteins. Arch Biochem Biophys. 1969 Feb;129(2):534–538. doi: 10.1016/0003-9861(69)90211-2. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES