Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1978-10-18
pubmed:abstractText
We have investigated a chloroform--methanol extracted material from electric organ of Torpedo marmorata with respect to binding of [3H]-acetyl-alpha-neurotoxin and [3H]-acetylcholine. No binding was observed which is in contrast to observations with detergent extracted receptor. Further, no crossreactivity could be demonstrated between the chloroform--methanol extracted proteolipid and antibodies against the detergent extracted receptor. Labelling in the membrane with [3H]-acetyl-alpha-neurotoxin before extraction with chloroform--methanol gave a very low yield of extracted labelled compound. The protein yield is about 0.3% of the total in the homogenate and only 0.04% of the specifically bound neurotoxin. Using the alkylating affinity label [3H]-N-propylbenzilylcholine mustard (1) and also [3H]-atropine, which both bind, at low concentrations, specifically to the muscarinic acetylcholine receptor, binding was studied to the chloroform--methanol extracted proteolipid from rat brain cortex. No specific binding could, however, be demonstrated. Prelabelling in the membrane with 1 and subsequent extraction with chloroform--methanol gave a protein yield of about 1% and an extraction of 26% of the specifically bound label.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0302-4369
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
370-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
Immunological and binding studies on chloroform--methanol extracts from electroplax of Torpedo marmorata and from rat brain cortex. Comparison of the material solubilized by organic solvents with the receptor proteins solubilized by detergents.
pubmed:publicationType
Journal Article, Comparative Study