Hostname: page-component-78c5997874-v9fdk Total loading time: 0 Render date: 2024-11-19T17:55:41.118Z Has data issue: false hasContentIssue false
  • English
  • Français

A glyco-phosphoprotein in human milk

Published online by Cambridge University Press:  01 June 2009

Norihiro Azuma  and
Kunio Yamauchi
Norihiro Azuma
Affiliation:
Department of Agricultural Chemistry, University of Tokyo, Bunkyo-ku, Tokyo 113, Japan
Kunio Yamauchi
Affiliation:
Department of Agricultural Chemistry, University of Tokyo, Bunkyo-ku, Tokyo 113, Japan
Get access Rights & Permissions [Opens in a new window]

Summary

A highly glycosylated phosphoprotein (HGPP) was isolated from a human casein fraction by reversed-phase high-performance liquid chromatography. This component contained carbohydrates to ∼ 38·2% (w/w) and phosphorus to ∼ 1·6% (w/w). The molecular weight of this HGPP as estimated by sodium dodecyl sulphate–polyacrylamide gel electrophoresis ∼ 41000. Ultracentrifugal analysis revealed that the sedimentation coefficient of the HGPP was 2·6S in a 10 mM-imidazole-HCl buffer at pH 7·0 and 27 °C, but this component interacted with human κ-casein and formed a complex with s = 10·4S.

Type
Original Articles
Information
Journal of Dairy Research , Volume 54 , Issue 2 , May 1987 , pp. 199 - 205
Copyright
Copyright © Proprietors of Journal of Dairy Research 1987

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

Azuma, N., Kadoya, H. & Yamauchi, K. 1985 a A 20,000-dalton casein fragment in human milk. Journal of Dairy Science 68 2176–2183CrossRefGoogle ScholarPubMed
Azuma, N., Kaminogawa, S. & Yamauchi, K. 1984 a Molecular weight and conformation of human κ-casein and its interaction with other human milk proteins. Agricultural and Biological Chemistry 48 771–776Google Scholar
Azuma, N., Kaminogawa, S. & Yamauchi, K. 1984 b Properties of glycomacropeptide and para-κ-casein derived from human κ-casein and comparison of human and bovine κ-caseins as to susceptibility to chymosin and pepsin. Agricultural and Biological Chemistry 48 2025–2031Google Scholar
Azuma, N., Kaminogawa, S. & Yamauchi, K. 1985 b Reconstitution of human casein micelle and its properties. Agricultural and Biological Chemistry 49 2655–2660Google Scholar
Azuma, N., Kobayashi, H. & Yamauchi, K. 1981 Variation in casein from individual human milk samples. Agricultural and Biological Chemistry 45 1007–1009Google Scholar
Bigklow, C. C. 1967 On the average hydrophobicity of proteins and the relation between it and protein structure. Journal of Theoretical Biology 16 187–211CrossRefGoogle Scholar
Clamp, J. R., Bhatti, T. & Chambers, R. E. 1972 The examination of carbohydrate in glycoproteins by gas-liquid chromatography. In Glycoproteins, 2nd edn Part A pp. 300–321 (Ed. Gottschalk, A.). Amsterdam: ElsevierGoogle ScholarPubMed
Green, M. R. 1983 Detection in milk of a 60,000 M r mouse and a 68,000 M r human phosphorylated glycoprotein by histochemical analysis on polyacrylamide gels. Journal of Histochemistry and Cytochemistry 31 709–716CrossRefGoogle Scholar
Greenberg, R. & Groves, M. L. 1984 Plasmin cleaves human β-casein. Biochemical and Biophysical Research Communications 125 463–468CrossRefGoogle ScholarPubMed
Heckman, A. 1971 Association of lactoferrin with other proteins as demonstrated by changes in electrophoretic mobility. Biochimica el Biophysica Acta 251 380–387CrossRefGoogle Scholar
Laemmli, U. K. 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 680–685CrossRefGoogle ScholarPubMed
Nagasawa, T., Kiyosawa, I. & Takase, M. 1974 Lactoferrin and serum albumin of human casein in colostrums and milk. Journal of Dairy Science 57 1159–1163CrossRefGoogle Scholar
Nagasawa, T., Ryoki, T., Kiyosawa, I. & Kuwahara, K. 1967 Studies on human casein. I. Fractionation of human casein by diethylaminoethyl cellulose column chromatography. Archives of Biochemistry and Biophysics 121 502–507CrossRefGoogle ScholarPubMed
Rousbr, G., Siakotos, A. N. & Fleicher, S. 1966 Quantitative analysis of phospholipids by TLC and phosphorus analysis of spots. Lipids 1 85–86Google Scholar
Slattery, C. W. 1981 A human casein with characteristics similar to bovine κ-casein. Purification and properties. Federation Proceedings 40 1565Google Scholar
Spiro, R. G. 1972 A study of the carbohydrate of glycoproteins. Methods in Enzymology 28 11–14Google Scholar
Weber, K. & Osborn, M. 1969 The reliability of molecular weight determinations by dodecyl sulfate- polyacrylamide gel electrophoresis. Journal of Biological Chemistry 244 4406–4412CrossRefGoogle ScholarPubMed
Yamauchi, K., Azuma, N., Kobayashi, H. & Kaminogawa, S. 1981 Isolation and properties of human κ-casein. Journal of Biochemistry 90 1005–1012CrossRefGoogle ScholarPubMed
Zaciiarius, R. M., Zell, T. E., Morrison, J. H. & Woodlock, J. J. 1969 Glycoprotein staining following electrophoresis on acrylamide gels. Analytical Biochemistry 30 148–152CrossRefGoogle Scholar