Opening book details…
Can I read The Phosphorylation Pattern of Human α~S1~‐casein Is Markedly Different from the Ruminant Species on EtoBox?
The Phosphorylation Pattern of Human α~S1~‐casein Is Markedly Different from the Ruminant Species by Esben S. Sørensen; Lise Møller; Maria Vinther; Torben E. Petersen; Lone K. Rasmussen is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
What is The Phosphorylation Pattern of Human α~S1~‐casein Is Markedly Different from the Ruminant Species about?
Caseins are highly phosphorylated milk proteins assembled in large colloidal structures termed micelles. In the milk of ruminants, α~s1~‐casein has been shown to be extensively phosphorylated. In this report we have determined the phosphorylation pattern of human α~s1~‐casein by a combination of matrix‐assisted laser desorption mass spectrometry and amino acid sequence analysis. Three phosphorylation variants were identified. A nonphosphorylated form, a variant phosphorylated at Ser18 and a variant phosphorylated at Ser18 and Ser26. Both phosphorylation sites are located in the amino acid recognition sequence of the mammary gland casein kinase. Notably, no phosphorylations were observed in the conserved region covering residues Ser70–Glu78, which is extensively phosphorylated in the ruminant α~s1~‐caseins.
Who reads The Phosphorylation Pattern of Human α~S1~‐casein Is Markedly Different from the Ruminant Species?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- Esben S. Sørensen; Lise Møller; Maria Vinther; Torben E. Petersen; Lone K. Rasmussen
- Publisher
- John Wiley and Sons; Springer; Wiley (Blackwell Publishing); Springer-Verlag; Blackwell Publishing Inc.; Springer Verlag; Wiley; Springer Science and Business Media LLC (ISSN 1432-1327)
- Published
- 2003
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Physical Sciences)