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A cyclic AMP‐dependent phosphorylation of spectrin dimer
Author(s) -
Lutz Hans U.
Publication year - 1984
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(84)80343-9
Subject(s) - spectrin , ankyrin , phosphorylation , band 3 , epb41 , dimer , chemistry , biochemistry , microbiology and biotechnology , biophysics , biology , cytoskeleton , membrane protein , membrane , gene , cell , organic chemistry
In contrast to the properties of spectrin obtained from [ 32 P]phosphate‐labeled red cells, purified spectrin dimer could be phosphorylated by a cAMP‐dependent protein kinase from bovine heart. Both spectrin bands were phosphorylated. Spectrin band 2 contained in addition to autophosphorylated peptides several phosphopeptides that were distinct from autophosphorylated ones. The cAMP‐dependent phosphorylation of spectrin band 1 was modulated by reducing agent and the concentration of spectrin. At high concentrations spectrin band 2 was predominantly labeled. The cAMP‐dependent phosphoform of spectrin band 2 had a p I slightly higher than that of autophosphorylated spectrin band 2, but lower than that of ankyrin.