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Science 27 April 1990:
Vol. 248. no. 4954, pp. 490 - 492
DOI: 10.1126/science.2158672
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Articles
Science, Vol 248, Issue 4954, 490-492
Copyright © 1990 by American Association for the Advancement of Science
Primary structure of the gamma subunit of the DHP-sensitive calcium channel from skeletal muscle
SD Jay,
SB Ellis,
AF McCue,
ME Williams,
TS Vedvick,
MM Harpold,
and
KP Campbell
Howard Hughes Medical Institute, University of Iowa College of Medicine, Iowa City 52242.
Affinity-purified, polyclonal antibodies to the gamma subunit of the dihydropyridine (DHP)-sensitive, voltage-dependent calcium channel have been used to isolate complementary DNAs to the rabbit skeletal muscle protein from an expression library. The deduced primary structure indicates that the gamma subunit is a 25,058-dalton protein that contains four transmembrane domains and two N-linked glycosylation sites, consistent with biochemical analyses showing that the gamma subunit is a glycosylated hydrophobic protein. Nucleic acid hybridization studies indicate that there is a 1200-nucleotide transcript in skeletal muscle but not in brain or heart. The gamma subunit may play a role in assembly, modulation, or the structure of the skeletal muscle calcium channel.
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