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A membrane‐bound protein kinase from mouse liver stimulated by iron
Author(s) -
Loeb Jacques E.,
Creuzet Claudine,
Komano Odile,
Boissel Jean-Paul
Publication year - 1983
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(83)80520-1
Subject(s) - phosphorylation , threonine , chemistry , divalent , in vitro , protein kinase a , protein phosphorylation , biochemistry , kinase , membrane , membrane protein , serine , organic chemistry
At μM levels, iron stimulates strongly the in vitro phosphorylation of a membrane protein from mouse liver. This phosphorylation also occurs in the absence of other added divalent cations but to a lower degree. In SDS gels the phosphorylated protein has app. M r 250 000 in the absence of mercaptoethanol and M r 130 000 in its presence. It is phosphorylated on threonine residues.