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Occurrence of γ-caseins in buffalo milk

Published online by Cambridge University Press:  01 June 2009

Patrick Trieu-Cuot  and
Francesco Addeo
Patrick Trieu-Cuot
Affiliation:
Laboratoire de Biochimie et Technologie Laitières, Institut National de la Recherche Agronomique, CNRZ, 78350 Jouy-en-Josas, France
Francesco Addeo
Affiliation:
Istituto di Industrie Agrarie dell'Università di Napoli, 80055 Portici∣, Naples, Italy
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Summary

Using polyacrylamide gel electrophoresis, 2-dimensional gel electrophoresis and electrofocusing, it has been shown that 4 basic fragments were produced by action of plasmin on buffalo β-casein. These fragments were present in whole buffalo casein prepared from bulk milk. Their mol. wts, 20000, 16000 and 11000 (2 components) were determined by SDS-gradient polyacrylamide gel electrophoresis. It is suggested that 3 of them are homologous to bovine γ1-, γ2- and γ3-caseins respectively, while the last one (mol. wt 16000), which has no counterpart in plasmin digest of bovine β-casein, could arise from a cleavage at bond 68–69.

Type
Original Articles
Information
Journal of Dairy Research , Volume 48 , Issue 2 , June 1981 , pp. 311 - 317
Copyright
Copyright © Proprietors of Journal of Dairy Research 1981

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References

REFERENCES

Addeo, F., Mercier, J. -C. & Ribadeau Dumas, B. (1977). Journal of Dairy Research 44, 455–468.CrossRefGoogle Scholar
Eigel, W. N. (1977). International Journal of Biochemistry 8, 187–192.CrossRefGoogle Scholar
Eigel, W. N., Hofmann, C. J., Chibber, B. A. K.Tomich, J. M.Keenan, T. W. & Mertz, E. T. (1979). Proceedings of National Academy of Sciences U.S.A. 76, 2244–2248.CrossRefGoogle Scholar
Gordon, W. G.Groves, M. L.Greenberg, R.Jones, S. B.Kalan, E. B., Peterson, R. F. & Townend, R. E. (1972). Journal of Dairy Science 55, 261–263.CrossRefGoogle Scholar
Groves, M. L.Gordon, W. G. (1969). Biochimica et Biophysica Acta 194, 421–432.CrossRefGoogle Scholar
Groves, M. L. & Kiddy, C. A. (1968). Archives of Biochemistry and Biophysics 126, 188–193.CrossRefGoogle Scholar
Kaminogawa, S.Mizobuchi, H. & Yamauchi, K. (1972). Agricultural and Biological Chemistry 36, 2163–2167.CrossRefGoogle Scholar
Petrilli, P.Chiansese, L. & Addeo, F. (1979). Journal of Dairy Research 46, 231–233.CrossRefGoogle Scholar
Ribadeac Dumas, B.Brignon, G.Grosclaude, F. & Mercier, J. -C. (1972). European Journal of Biochemistry 25. 505–514.CrossRefGoogle Scholar
Sherry, S.Alkjaersig, N. & Fletcher, A. P. (1966). Thrombosis et Diathesis Haemorrhagica 16, 18–31.Google Scholar
Trieu-Cuot, P. & Gripon, J. -C. (1981). Journal of Dairy Research, 48.Google Scholar
Uriel, J. (1966). Bulletin de la Société de Chimie Biologique 48, 969–982.Google Scholar
Waehseldt, T. V. (1975). BioSystems 6, 176–187.CrossRefGoogle Scholar