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Occurrence of five αs1-casein variants in ovine milk

Published online by Cambridge University Press:  01 June 2009

Lina Chianese ,
Giuseppina Garro ,
Rosalba Mauriello ,
Pasquale Laezza ,
Pasquale Ferranti  and
Francesco Addeo
Lina Chianese
Affiliation:
Dipartimento di Scienza degli Alimenti, Universitá degli Studi di Napoli Federico II, Parco Gussone, 1-80055 Portici, Italia
Giuseppina Garro
Affiliation:
Dipartimento di Scienza degli Alimenti, Universitá degli Studi di Napoli Federico II, Parco Gussone, 1-80055 Portici, Italia
Rosalba Mauriello
Affiliation:
Dipartimento di Scienza degli Alimenti, Universitá degli Studi di Napoli Federico II, Parco Gussone, 1-80055 Portici, Italia
Pasquale Laezza
Affiliation:
Dipartimento di Scienza degli Alimenti, Universitá degli Studi di Napoli Federico II, Parco Gussone, 1-80055 Portici, Italia
Pasquale Ferranti
Affiliation:
Dipartimento di Scienza degli Alimenti, Universitá degli Studi di Napoli Federico II, Parco Gussone, 1-80055 Portici, Italia
Francesco Addeo
Affiliation:
Istituto Sperimentale Lattiero-Caseario, Via A. Lombardo 11, 1-20075 Lodi, Italia
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Summary

Five ovine αsl-casein variants (A–E) were identified in an Italian population sample using gel electrophoresis at alkaline pH, gel isoelectric focusing, two dimensional gel electrophoresis, and immunoblotting with polyclonal antibodies against αs1-casein. Each casein sample produced two peaks by fast reversed-phase HPLC. Gel isoelectric focusing and electrospray mass spectrometry were used to demonstrate that the first HPLC peak contained the 191 residue αsl-casein molecular species and the second the 199 residue species, in proportions of ∼20:80. Only in the case of the sample containing αsl-casein CE was the method for the separation of the single short and long forms of each variant unsuccessful. Both two dimensional electrophoresis followed by staining with polyclonal antibodies against αsl-casein and electrospray mass spectrometry showed a heterogeneity consistent with that expected from a protein chain with three levels of phosphorylation and two different lengths. However, especially for αsl-caseins D and E, a further uncharacterized heterogeneity was detected.

Type
Original Articles
Information
Journal of Dairy Research , Volume 63 , Issue 1 , February 1996 , pp. 49 - 59
Copyright
Copyright © Proprietors of Journal of Dairy Research 1996

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References

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