Abstract
The E variant of bovine β-casein differs from the reference βA 2 variant by the substitution 36 Glu (βA 2) → Lys (βE). Seryl residue 35 is phosphorylated in βE as in βA 2. The variant βE can be compared to the variant βC which also differs from βA 2 by a Glu → Lys substitution. However, this substitution then affects the position 37, and, in this case, the seryl residue 35 is not phosphorylated. These observations tend to support the existence of the phosphorylation code of bovine caseins as postulated by Mercier et al. [1].
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