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Two physiological substrate‐specific casein kinases are present in the bovine mammary gland
Author(s) -
Brooks Charles L.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80167-x
Subject(s) - casein kinase 2 , casein kinase 1 , casein kinase 2, alpha 1 , casein , phosphorylation , kinase , biochemistry , chemistry , dephosphorylation , protein kinase a , biology , cyclin dependent kinase 2 , phosphatase
Two species of casein kinase from lactating bovine mammary gland have been identified; a Ca 2+ ‐ and CM‐independent casein kinase and a Ca 2+ ‐ and CM‐dependent casein kinase. The Ca 2+ ‐ and CM‐independent casein kinase phosphorylates previously dephosphorylated α s1 ‐, β‐ or κ‐casein while the Ca 2+ ‐ and CM‐dependent casein kinase prefers previously dephosphorylated β‐ or κ‐casein as substrates. Two activities are indicated by their substrate specificity, sensitivity to Ca 2+ and CM, pH maxima, and differential solubilization by anionic detergents. The presence of a regulated casein kinase in the lactating mammary gland suggests that casein phosphorylation may be a regulator of micelle formation or secretion.