Characterization of DHP binding protein in crayfish striated muscle

FEBS Letters

Novotova, M.¹  Zachar, J.¹  Krizanova, O.¹ 

[1] Institute of Molecular Physiology and Genetics, Slovak Academy of Sciences, Vlarska 5, 833 34 Bratislava, Czechoslovakia

关键词: Crayfish;    Calcium channel;    Ca2+ antagonist;    E-C;    excitation-contraction;    WGA;    wheat germ agglutinin;    Chaps;    3-(3-cholamidopropyl)-dimethyl-ammonio-l-propanesulfonate;    DHP;    dihydropyridine;    SDS;    sodium dodecyl sulphate;   

DOI  :  10.1016/0014-5793(90)80951-E

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The dihydropyridine calcium channel blocker, [³H]PN 200-110, binds specifically also to crayfish muscle membranes, though with a binding capacity smaller than that measured with rabbit or human skeletal muscle membranes. [³H]PN 200-110 binding proteins from the crayfish T-tubules were solubilized and purified on WGA Sepharose or extracted from gel. The purified protein has a molecular mass of approximately 190 kDa under nonreducing conditions and was able to transport calcium after reconstitution. Polyclonal antibodies against crayfish T-tubules enriched with purified DHP-binding protein were shown to bind to DHP-binding protein from both the crayfish and the rabbit skeletal muscle, although not with the same intensity. Electron microscopy showed the presence of ovoid particles. Our results suggest that a voltage-dependent calcium channel may be present in crayfish skeletal muscle, which is homological with the L-type calcium channel in rabbit skeletal muscle.

【 授权许可】

Unknown