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

Albert T Leung; Toshiaki Imagawa; Kevin P Campbell

doi:10.1016/S0021-9258(18)47507-2

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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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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

Albert T Leung, Toshiaki Imagawa and Kevin P Campbell

The Journal of biological chemistry, Vol.262(17), pp.7943-7946

1987

DOI: 10.1016/S0021-9258(18)47507-2

PMID: 2439496

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Abstract

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.

Cell Physiology

Fundamental and applied biological sciences. Psychology

Biological and medical sciences

Molecular and cellular biology

Muscle contraction

Details

Title: Subtitle: 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
Creators: Albert T Leung - Univ. Iowa, dep. physiology & biophysics, Iowa City IA 52242, United States
Toshiaki Imagawa - Univ. Iowa, dep. physiology & biophysics, Iowa City IA 52242, United States
Kevin P Campbell - Univ. Iowa, dep. physiology & biophysics, Iowa City IA 52242, United States
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.262(17), pp.7943-7946
DOI: 10.1016/S0021-9258(18)47507-2
PMID: 2439496
NLM abbreviation: J Biol Chem
ISSN: 0021-9258
eISSN: 1083-351X
Publisher: American Society for Biochemistry and Molecular Biology; Bethesda, MD
Language: English
Date published: 1987
Academic Unit: Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute
Record Identifier: 9984068368902771

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