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PMID: 2436616 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Evidence for a junctional feet-ryanodine receptor complex from sarcoplasmic reticulum.

Biochemical and biophysical research communications ·Vol. 143 ·No. 2 ·1987-03-13 ·Pages 704-9

Lai FA, Erickson H, Block BA, Meissner G

Abstract

Heavy sarcoplasmic reticulum vesicles, labelled with the Ca2+ release channel probe [3H]ryanodine, were solubilized in detergent, then centrifuged through sucrose gradients. A single peak of ryanodine binding activity was observed with an apparent sedimentation coefficient of 30S. Electron microscopy of the peak fraction showed disk structures of 25-28 nm diameter and 10 nm thickness. Proteins specifically enriched in the peak fraction were the Mr 160,000 and 260,000 and junctional feet proteins (Mr 320,000 and 300,000). This suggests that the feet proteins and ryanodine receptor may be specifically associated into a large oligomeric complex comprising subunits of Mr 160,000-320,000.

MeSH Terms
Alkaloids/metabolism Animals Calcium/physiology Intracellular Membranes/metabolism,ultrastructure Ion Channels/metabolism Microscopy, Electron Rabbits Receptors, Cholinergic/metabolism Ryanodine/metabolism Ryanodine Receptor Calcium Release Channel Sarcoplasmic Reticulum/metabolism,ultrastructure
Chemicals
Alkaloids Ion Channels Receptors, Cholinergic Ryanodine Receptor Calcium Release Channel Ryanodine Calcium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Lai F A
Erickson H
Block B A
Meissner G
Article Info
Journal
Biochemical and biophysical research communications
Abbr.
Biochem Biophys Res Commun
ISSN
0006-291X
Published
1987-03-13
Pages
704-9
Language
English
Region
United States
NLM ID
0372516
Subset
IM
Grants
NIADDK NIH HHS · AM 18687 · United States
NIGMS NIH HHS · GM 28553 · United States
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