Biochemical and ultrastructural characterization of the 1,4-dihydropyridine receptor from rabbit skeletal muscle. Evidence for a 52,000 Da subunit

Albert T Leung; Toshiaki Imagawa; Barbara Block; Clara Franzini-Armstrong; Kevin P Campbell

doi:10.1016/S0021-9258(19)35451-1

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Biochemical and ultrastructural characterization of the 1,4-dihydropyridine receptor from rabbit skeletal muscle. Evidence for a 52,000 Da subunit

Journal article

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Biochemical and ultrastructural characterization of the 1,4-dihydropyridine receptor from rabbit skeletal muscle. Evidence for a 52,000 Da subunit

Albert T Leung, Toshiaki Imagawa, Barbara Block, Clara Franzini-Armstrong and Kevin P Campbell

The Journal of biological chemistry, Vol.263(2), pp.994-1001

01/15/1988

DOI: 10.1016/S0021-9258(19)35451-1

PMID: 2826471

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Abstract

The 1,4-dihydropyridine receptor purified from rabbit skeletal muscle contains four polypeptide components of 175,000 Da (nonreduced)/150,000 Da (reduced), 170,000, 52,000, and 32,000 Da (Leung, A. T., Imagawa, T., and Campbell, K. P. (1987) J. Biol. Chem. 262, 7943-7946). A monoclonal antibody specific to the 52,000-Da polypeptide component of the dihydropyridine receptor has been produced and used in immunoprecipitation and immunoblotting experiments to demonstrate that the 52,000-Da polypeptide is an integral subunit of the purified dihydropyridine receptor. Peptide mapping experiments with 32P-labeled dihydropyridine receptor have also demonstrated that the 52,000-Da polypeptide is distinct from and not a proteolytic fragment of the 170,000-Da subunit. Densitometric scanning of Coomassie Blue-stained sodium dodecyl sulfate-polyacrylamide gels of the purified dihydropyridine receptor has demonstrated that the 52,000-Da polypeptide exists in a 1:1 stoichiometric ratio with the 170,000-, 175,000/150,000-, and 32,000-Da subunits of the dihydropyridine receptor. Electron microscopy of the freeze-dried, rotary-shadowed dihydropyridine receptor has shown that the preparation contains a homogeneous population of 16 x 22-nm ovoidal particles large enough to contain all four polypeptides of the dihydropyridine receptor. The particles have two distinct components of similar size which may represent the location in the molecule of the two larger subunits.

Phosphorylation

Rabbits

Receptors, Nicotinic - metabolism

Animals

Molecular Weight

Calcium Channels

Peptide Mapping

Antibodies, Monoclonal

Microscopy, Electron

Muscles - metabolism

Macromolecular Substances

Details

Title: Subtitle: Biochemical and ultrastructural characterization of the 1,4-dihydropyridine receptor from rabbit skeletal muscle. Evidence for a 52,000 Da subunit
Creators: Albert T Leung - Department of Physiology and Biophysics, University of Iowa, Iowa City 52242
Toshiaki Imagawa
Barbara Block
Clara Franzini-Armstrong
Kevin P Campbell
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.263(2), pp.994-1001
DOI: 10.1016/S0021-9258(19)35451-1
PMID: 2826471
NLM abbreviation: J Biol Chem
ISSN: 0021-9258
eISSN: 1083-351X
Publisher: United States
Grant note: HL-15835 / NHLBI NIH HHS HL-37187 / NHLBI NIH HHS
Language: English
Date published: 01/15/1988
Academic Unit: Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute
Record Identifier: 9984068259502771

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