期刊论文详细信息
FEBS Letters
Identification of a new 84/82 kDa calmodulin‐binding protein, which also interacts with actin filaments, tubulin and spectrin, as synapsin I
Sobue, Kenji1  Okabe, Toshio1 
[1] Department of Neurochemistry and Neuropharmacology, Institute of Higher Nervous Activity, Osaka University Medical School, 4-3-57 Nakanoshima, Kita-ku, Osaka 530, Japan
关键词: Calmodulin-binding protein;    Synapsin I;    Actin filament;    Tubulin;    Spectrin;    Ca2+ dependence;    Calmodulin dependence;    Kinase II;   
DOI  :  10.1016/0014-5793(87)81488-6
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

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 Ca2-dependent, and was inhibited by trifluoperazine, the association constant being calculated to be 2.2 × 106 M−1. Maximally, 1 mol of calmodulin bound to 1 mol of the purified protein. This protein was phosphorylated by both kinase II (Ca2+- 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.

【 授权许可】

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