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Role of mammary casein kinase in the phosphorylation of milk proteins

Published online by Cambridge University Press:  01 June 2009

Elizabeth W. Bingham
Elizabeth W. Bingham
Affiliation:
Eastern Regional Research Center*, Philadelphia, Pennsylvania 19118, USA
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Summary

Casein kinase from lactating bovine mammary gland catalyses the transfer of the terminal phosphoryl group of ATP to specific serine residues in dephosphorylated caseins. Best substrates for casein kinase are the dephosphorylated proteins (bovine αs1 - and β-caseins and pepsin), unphosphorylated human β-casein and the dephosphorylated peptide (residues 1–25) from bovine β-casein. Results obtained with bovine and human β-caseins indicate that the two serines underlined in the cluster Ser-Leu-Ser-Ser-Ser are particularly susceptible to the action of casein kinase. Since a similar sequence is found in dephosphorylated αs1-casein, it is probable that serines in this region of αs1-casein are also phosphorylated. The results support the concept that certain serines in casein are particularly susceptible to phosphorylation by casein kinase.

Type
Section A. Biological Aspects of Milk Proteins
Information
Journal of Dairy Research , Volume 46 , Issue 2: Symposium on the Physics and Chemistry of Milk Proteins , April 1979 , pp. 181 - 185
Copyright
Copyright © Proprietors of Journal of Dairy Research 1979

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References

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