The acetylcholine receptor protein from human muscle was extracted with the non-ionic detergent Triton X-100 and purified by affinity chromatography on a-Naja toxin sepharose 4B. Further purification on Dicap-MP sepharose 4B, a choline analog compound, led to ACHR preparations with specific activiti
Immunological studies of acetylcholine receptors
β Scribed by Lindstrom, Jon
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1976
- Tongue
- English
- Weight
- 699 KB
- Volume
- 4
- Category
- Article
- ISSN
- 0091-7419
No coin nor oath required. For personal study only.
β¦ Synopsis
Abstract
Immunochemical techniques for the study of acetylcholine receptors are described. Immunization of rabbits, rats, guinea pigs, and goats with acetylcholine receptor protein purified from Electrophorus electric organ tissue results in muscular weakness and death due to impaired neuromuscular transmission. Serum from immunized animals contains high concentrations of antibodies directed at receptors from the electric organ and low concentrations of antibodies directed at receptors from skeletal muscle. The detailed similarities between the disease of receptorβimmunized animals, βexperimental autoimmune myasthenia gravisβ (EAMG), and myasthenia gravis are compared. Reactions of antisera from animal with EAMG with receptor from Electrophorus and Torpedo are studied. Antireceptor antibodies in these antisera are directed predominantly at determinants other than the acetylcholineβbinding site.
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## Abstract The response of human T lymphocytes against the nicotinic acetylcholine receptor (AChR) was studied in five patients with myasthenia gravis (MG) and in six healthy donors using either native Torpedo AChR or recombinant protein derived from the mammalian AChR Ξ± subunit (X4, residues 6β21