Linked Life Data

8508306

Source:http://linkedlifedata.com/resource/pubmed/id/8508306

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1993-7-15
pubmed:abstractText
We show that in the central nervous system of the fly, Drosophila melanogaster, choline acetyltransferase (ChAT) activity exists under two molecular forms, a soluble, hydrophilic form and a membrane-bound, amphiphilic form. This is based on the following demonstrations of differential solubilization and interaction with non-denaturing detergents: sequential extraction of Drosophila heads produced low-salt-soluble (83-87%) and detergent-soluble (6-7%) ChAT activity. Sedimentation in sucrose gradients of detergent-soluble ChAT was found to be influenced by the type of detergent present in the gradient (Triton X-100 and Brij 96). This was not the case for low-salt-soluble ChAT. To further confirm these findings, we subjected Drosophila heads to Triton X-114 fractionation. This method, which yielded 12% of amphiphilic ChAT activity, separates hydrophilic from amphiphilic proteins. Compared to central nervous tissue of rat and Torpedo electric lobes, Drosophila head contained the highest proportion of amphiphilic ChAT activity. Synaptosomes isolated from Torpedo electric organ exhibited higher levels of amphiphilic ChAT than did electric lobes. Of the three animal species analyzed here, the Torpedo amphiphilic enzyme was the most hydrophobic and the rat enzyme the least hydrophobic. The proportion of amphiphilic ChAT was analyzed during Drosophila development. The percentage of this activity increased about 7 times from embryo to larva and then remained constant until the adult fly age.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-8993
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
609
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
223-30
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
The proportion of amphiphilic choline acetyltransferase in Drosophila melanogaster is higher than in rat or Torpedo and is developmentally regulated.
pubmed:affiliation
Department of Pharmacology, Centre Médical Universitaire, Geneva, Switzerland.
pubmed:publicationType
Journal Article, Comparative Study, In Vitro, Research Support, Non-U.S. Gov't