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Characterization of DHP binding protein in crayfish striated muscle
Author(s) -
Krizanova O.,
Novotova M.,
Zachar J.
Publication year - 1990
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(90)80951-e
Subject(s) - crayfish , skeletal muscle , polyclonal antibodies , calcium , binding protein , biochemistry , biology , dihydropyridine , calcium channel , binding site , biophysics , chemistry , microbiology and biotechnology , anatomy , antibody , organic chemistry , fishery , gene , immunology
The dihydropyridine calcium channel blocker, [ 3 H]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. [ 3 H]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.