Linked Life Data

6527362

Source:http://linkedlifedata.com/resource/pubmed/id/6527362

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1985-4-5
pubmed:abstractText
The nicotinic acetylcholine receptor (AcChR) has been purified from both the electric organ and the muscle of the fish Electrophorus electricus. Upon SDS gel electrophoresis muscle AcChRs appeared to contain four main polypeptides whose molecular weights were similar but not identical to the molecular weights of the four peptides present in the electric organ AcChR. Each of these peptides has been isolated and their amino-terminal sequences have been determined. The AcChRs from muscle were found to be composed of four homologous proteins of apparent molecular weight 40,500, 50,000, 56,000 and 63,000, respectively. The subunit of Mr 40,500 is present in two copies for each AcChR molecule, while the other three components are present in one copy. No difference was found between the sequenced segments of corresponding subunits from muscle and from electric organ AcChR, suggesting that AcChRs in different tissues of the same animal are products of identical genes. The Electrophorus AcChR subunits are highly homologous with the corresponding subunits of Torpedo californica AcChR.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0197-5110
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
801-16
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Multisubunit structure and amino-terminal sequences of piscine muscle acetylcholine receptor.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't