Published December 17, 1982
| public
Journal Article
Mammalian Muscle Acetylcholine Receptor: A Supramolecular Structure Formed by Four Related Proteins
Abstract
The nicotinic acetylcholine receptor has been purified from fetal calf muscle. Amino terminal amino acid sequence data indicate that the mammalian receptor is formed from closely related but distinct subunits. A cytoskeletal component, actin, may be associated with the receptor.
Additional Information
© 1982 American Association for the Advancement of Science. Received 24 May 1982; revised 24 September 1982. This research was supported by USPHS NS-10294 and GM-06965 and by grants from the Muscular Dystrophy Association of America, the Myasthenia Gravis Foundation (Los Angeles Chapter), the Pew Charitable Trust, and the Weingart Foundation. We thank John Racs and Laurie Jutzi for technical assistance.Additional details
- Eprint ID
- 53922
- Resolver ID
- CaltechAUTHORS:20150121-084336620
- NS-10294
- U. S. Public Health Service (USPHS)
- GM-06965
- U. S. Public Health Service (USPHS)
- Muscular Dystrophy Association of America
- Myasthenia Gravis Foundation
- Pew Charitable Trust
- Weingart Foundation
- Created
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2015-01-21Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field