Linked Life Data

6413654

Source:http://linkedlifedata.com/resource/pubmed/id/6413654

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1983-11-23
pubmed:abstractText
Two distinct classes of acetylcholinesterase (AChE) from the fruit fly Drosophila melanogaster are reported: a soluble species that shows heterogeneity of forms and a particulate species. The subunit composition of the particulate enzyme was studied using the active site label [3H]diisopropylfluorophosphate. Comparison of the electrophoretic patterns on nondenaturing gels using the activity stain and the active site label shows that the label is specific to AChE. The smallest active site-containing subunit of the enzyme is a monomer of approximately 60,000 daltons MW. Two such units are linked by disulphide bonds to produce a dimer of about 110,000 daltons. Another monomeric form of MW approximately 64,000 daltons, although present, does not participate in the dimerisation. The particulate enzyme when solubilised exists as a 9-10S species as determined by sucrose gradient centrifugation. This species has a MW greater than 200,000, as shown by its behaviour on a coarse-bead Sephadex-G200 column. Electrophoretic analysis suggests a MW of nearly 250,000 daltons for this form. Thus, this species is likely to be a tetramer. One possibility is that this tetramer is made up of two units of 64,000 daltons each and a dimer of 110,000 daltons. Preliminary data on mutant enzymes that support such a possibility are also presented.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-3042
pubmed:author
pubmed:issnType
Print
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1243-52
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Molecular properties of Drosophila acetylcholinesterase.
pubmed:publicationType
Journal Article