Linked Life Data

567492

Source:http://linkedlifedata.com/resource/pubmed/id/567492

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1978-11-27
pubmed:abstractText
11-S acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) purified by affinity chromatography of trypsin-digested homogenates was shown to be contaminated with three other active forms of enzyme. The initial purification used an affinity column of the inhibitor, N-methylacridinium ion. Chromatography of the "affinity-pure" sample on hydroxyapatite resulted in two peaks of acetylcholinesterase activity. One peak contained only a form sedimenting at 11-S (approx. 85% of the recovered activity). The other peak consisted of a 9.5-S form, in addition to 14-S and 18-S forms. The 9.5-S form (approx. 7% of the activity) co-electrophoresed with 11-S in 6% polyacrylamide gels and co-sedimented with the same form in sucrose density gradients containing 0.1 M NaCl. The purified 11-S enzyme was shown to be homogeneous by sucrose density gradient centrifugation and electrophoresis. These results indicate that 11-S acetylcholinesterase may be unsuitable for some characterization studies due to undetected contamination by the 9.5-S form.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
525
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
112-21
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
On the homogeneity of 11-S acetylcholinesterase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.