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J. Biol. Chem., Vol. 262, Issue 17, 7943-7946, 06, 1987
AT Leung, T Imagawa and KP Campbell
The 1,4-dihydropyridine receptor purified from rabbit skeletal muscle
triads was shown to contain four protein components of 175,000, 170,000,
52,000, and 32,000 Da when analyzed by sodium dodecyl sulfate-
polyacrylamide gel electrophoresis under nonreducing conditions. Monoclonal
antibodies capable of specifically immunoprecipitating the
[3H]PN200-110-labeled dihydropyridine receptor from digitonin- solubilized
triads recognized the 170,000-Da protein on nitrocellulose transfers of
skeletal muscle triads, transverse tubular membranes, and purified
dihydropyridine receptor. Wheat germ agglutinin peroxidase stained the
175,000-Da protein on similar nitrocellulose transfers, demonstrating that
the 175,000-Da protein is the glycoprotein subunit of the purified
dihydropyridine receptor. The apparent molecular weight of the Mr 170,000
protein remained unchanged with reduction, whereas the apparent molecular
weight of the glycoprotein subunit shifted from 175,000 to 150,000 upon
reduction. These results demonstrate that the 1,4-dihydropyridine receptor
of the voltage-dependent Ca2+ channel from rabbit skeletal muscle contains
two distinct high molecular weight subunits of 175,000 and 170,000.
Structural characterization of the 1,4-dihydropyridine receptor of the voltage-dependent Ca2+ channel from rabbit skeletal muscle. Evidence for two distinct high molecular weight subunits
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