Linked Life Data

536451

Source:http://linkedlifedata.com/resource/pubmed/id/536451

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1980-5-14
pubmed:abstractText
The acetylcholinesterase was purified by CM-Sephadex chromatography and affinity chromatography on Sepharose bound m-[6-(6-aminocaproylamino)caproylamino]phenyltrimethylammonium bromide. The purified enzyme was obtained with a specific activity of 5470 U/mg (1160-fold purification) and a 89% yield. The molecular weight of the native enzyme was estimated to be 144,000. The enzyme is split into two subunits of approximately equal molecular weight (Mr 69,000) by SDS treatment. It is a glycoprotein and can be resolved by disc gel electrophoresis into seven and by isoelectric focusing into more than ten multiple forms. The N-terminal amino acid is serine.
pubmed:language
ger
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9673
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
177
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
99-107
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
[Purification by affinity chromatography and properties of the acetylcholinesterase of formosan cobra (Naja naja atra) venom (author's transl)].
pubmed:publicationType
Journal Article, English Abstract