Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1985-8-5
pubmed:abstractText
In the caudate nucleus of the species tested about 20% of the acetylcholinesterase was salt soluble and sedimented in sucrose density gradient centrifugation as monomeric 5 S and tetrameric 10 S enzyme. About 80% was solubilized by micellar concentrations of Triton X-100 and sedimented as a tetrameric 10 S species in the presence of detergent but formed aggregates in the absence thereof. All the enzyme displayed poor cross-reactivity with a precipitating assay (Ouchterlony) but in a solid phase non-precipitating assay the cross-reactivity could be quantified and ranged from 96 to less than 1% depending on the species.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0742-8413
pubmed:author
pubmed:issnType
Print
pubmed:volume
80
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
263-8
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Polymorphism and immunochemical cross-reactivity of acetylcholinesterases from the brains of human, dog, hog, bovine and horse.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't