Premium
Identification of a new 84/82 kDa calmodulin‐binding protein, which also interacts with actin filaments, tubulin and spectrin, as synapsin I
Author(s) -
Okabe Toshio,
Sobue Kenji
Publication year - 1987
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(87)81488-6
Subject(s) - spectrin , calmodulin , synapsin i , tubulin , actin , actin binding protein , calmodulin binding proteins , cytoskeleton , identification (biology) , binding protein , chemistry , microbiology and biotechnology , ef hand , biochemistry , biology , microtubule , actin cytoskeleton , gene , cell , membrane , vesicle , synaptic vesicle , enzyme , botany
A new 84/82 kDa calmodulin‐binding protein, which also interacts with actin filaments, tubulin and spectrin, was purified from the bovine synaptosomal membrane. The binding of calmodulin to this protein was Ca 2 ‐dependent, and was inhibited by trifluoperazine, the association constant being calculated to be 2.2 × 10 6 M −1 . Maximally, 1 mol of calmodulin bound to 1 mol of the purified protein. This protein was phosphorylated by both kinase II (Ca 2+ ‐ and calmodulin‐dependent kinase) and cyclic AMP‐dependent kinase. In addition, antibody against this protein was demonstrated to have an immunological crossreactivity with synapsin I in the synaptosomal membrane.