Hostname: page-component-68945f75b7-76l5x Total loading time: 0 Render date: 2024-08-05T16:38:40.624Z Has data issue: false hasContentIssue false
  • English
  • Français

Fractionation of bovine caseins by reverse phase high performance liquid chromatography: identification of a genetic variant

Published online by Cambridge University Press:  01 June 2009

Christophe Carles
Christophe Carles
Affiliation:
Laboratoire de Biochimie el Technologie Laitières, Institut National de la Recherche Agronomique, CNRZ, 78350 Jouy-en-Josas, France
Get access Rights & Permissions [Opens in a new window]

Summary

Samples of reduced whole casein from genetically typed individual cows were quantitatively separated into their main components, αsl-, αs2-, β- and κ-caseins by reverse phase high performance liquid chromatography (RP-HPLC) using a mobile phase of phosphate-buffered aqueous propan-2-ol containing sodium dodecyl sulphate and an octadecylsilyl stationary phase. One casein sample was found to give two peaks of β-casein of approximately equal areas. RP-HPLC of tryptic digests of the two separated peak fractions gave identical patterns with the exception of one peptide peak with different retention times. Amino acid analyses performed on both fractions showed that they corresponded to peptide 114–169 of β-casein A1. The atypical β-casein differed from the typical one by a Pro→Leu substitution in region 114–169.

Type
Original Articles
Information
Journal of Dairy Research , Volume 53 , Issue 1 , February 1986 , pp. 35 - 41
Copyright
Copyright © Proprietors of Journal of Dairy Research 1986

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

Gripon, J. C., Desmazeaud, M. J., Le Bars, D. & Bergère, J. L. 1975 [Study of the role of microorganisms and enzymes during cheese ripening. II. Effect of commercial rennet.] Lait 55 502–516CrossRefGoogle Scholar
Grosclaude, F., Mahè, M. F., Mercier, J. C. & Ribadeau-Dumas, B. 1972 [Characterization of the genetic variants of bovine αsl- and β-caseins.] European Journal of Biochemistry 26 328–337CrossRefGoogle Scholar
Mercier, J. C., Maubois, J. L., Poznanski, S. & Ribadeau-Dumas, B. 1968 [Preparative fractionation of cow and ewe caseins by chromatography on DEAE cellulose in the presence of urea and 2-mercaptoethanol.] Bulletin de la Sociètè de Chimie Biologique 50 521–530.Google Scholar
Ribadeau-Dumas, B., Brignon, G., Grosclaude, F. & Mercier, J. C. 1972 [Primary structure of bovine β-casein.] European Journal of Biochemistry 25 505–514.CrossRefGoogle ScholarPubMed
Swaisgood, H. E. 1982 Chemistry of milk protein. In Developments in Dairy Chemistry Vol. 1. Proteins pp. 1–59 (Ed. Fox, P. F.) London: Applied Science PublishersGoogle Scholar
Trieu-Cuot, P. & Gripon, J. C. 1981 Electrofocusing and twodimensional electrophoresis of bovine caseins. Journal of Dairy Research 48 303–310CrossRefGoogle Scholar