Hostname: page-component-586b7cd67f-r5fsc Total loading time: 0 Render date: 2024-11-30T15:17:30.344Z Has data issue: false hasContentIssue false

Electrofocusing and two-dimensional electrophoresis of bovine caseins

Published online by Cambridge University Press:  01 June 2009

Patrick Trieu-Cuot
Affiliation:
Laboratoire de Biochimie et Technologie Laitières, Institut National de la Recherche Agronomique CNRZ, 78350 Jouy-en-Josas, France
Jean-Claude Gripon
Affiliation:
Laboratoire de Biochimie et Technologie Laitières, Institut National de la Recherche Agronomique CNRZ, 78350 Jouy-en-Josas, France

Summary

The main components of bovine whole casein were characterized by electrofocusing; pi values of αs1-, β-, κ-, γ1-, γ2- and γ3-caseins were determined. A further identification of casein components was achieved by a 2-dimensional electrophoresis study. 2-Dimensional patterns of γ-caseins obtained from a hydrolysate of β-cascin by bovine plasmin are in good agreement with those of γ-caseins naturally present in whole casein.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1981

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

Andrews, A. T. (1978 a). European Journal of Biochemistry 90. 6771.CrossRefGoogle Scholar
Andrews, A. T. (1978 b). European Journal of Biochemistry 90, 5965.CrossRefGoogle Scholar
Blakeslev, R. W. & Boezi, J. A. (1977). Analytical Biochemistry 82, 580582.CrossRefGoogle Scholar
Brignon, G., Ribadeau Dumas, B. & Mercier, J. -C. (1976). FEBS Letters 71, 111116.CrossRefGoogle Scholar
Eigel, W. N. (1977). International Journal of Biochemistry 8, 187192.CrossRefGoogle Scholar
Eigel, W. N. & Keenan, T. W. (1979). International Journal of Biochemistry 10, 529535.CrossRefGoogle Scholar
Garnier, J., Mocquot, G., Ribadeau-Dumas, B. & Maibois, J. -L. (1968). Annales de la Sutrition et de I'Alimentation 22, B495–B552.Google Scholar
Gelsema, W. J., De Ligny, C. L. & Van Der veen, N. G. (1979). Journal of Chromatography 171, 171181.CrossRefGoogle Scholar
Gripon, J. C., Desmazeaud, M. J., Le Bars, D. & Bergère, J. L. (1975). Lait 55, 502516.CrossRefGoogle Scholar
Josephson, R. V. (1972). Journal of Dairy Science 55, 15351543.CrossRefGoogle Scholar
Josephson, R. V., Maheswaran, S. K., Morr, C. V., Jenness, R. & Lindorfer, R. K. (1971). Analytical Biochemistry 40. 476482.CrossRefGoogle Scholar
Laemmli, U. K. (1970). Nature 227, 680685.CrossRefGoogle Scholar
Manson, W., Carolan, T. & Annan, W. D. (1977). European Journal of Biochemistry 78, 411417.CrossRefGoogle Scholar
Mercier, J. -C., Maubois, J. -L., Poznanski, S. & Ribadeau-Dumas, B. (1968). Bulletin de la Société de Chimie Biologique 50, 521530.Google Scholar
Nelson, C. A. (1971). Journal of Biological Chemistry 246, 38953901.CrossRefGoogle Scholar
Ribadeau Dumas, B., Brignon, G., Grosclaude, F. & Mercier, J. -C. (1972). European Journal of Biochemistry 25, 505514.CrossRefGoogle Scholar
Scheele, G. A. (1975). Journal of Biological Chemistry 250, 53755385.CrossRefGoogle Scholar
Studier, F. W. (1973). Journal of Molecular Biology 79, 237248.CrossRefGoogle Scholar
Ui, N. (1971). Biochimica et Biophysica Ada 229, 567581.Google Scholar
Uriel, J. (1966). Bulletin de la Société de Chimie Biologique 48, 969982.Google Scholar