Linked Life Data

2916838

Source:http://linkedlifedata.com/resource/pubmed/id/2916838

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-3-16
pubmed:abstractText
The concentration dependences of the activities of cytochalasin B, D, E, and H in capping and cleaving actin filaments have been assayed using fluorescence photobleaching recovery. Filament capping was detected by the increase in mobile G-actin. Cytochalasin D (CD) showed the strongest filament capping activity, with an apparent dissociation constant from filament ends of 50 nM. The order of capping activity was CD greater than CH greater than CE much greater than CB. Filament cleavage was detected by the increase in the diffusion coefficients of actin filaments. By this criterion the order of filament cleavage activity was CD, CE greater than CH much greater than CB. Cytochalasin B shows some activity in cleavage of filaments over a concentration range (0-100 microM) at which it shows no appreciable capping activity. This activity, together with results from other groups, is interpreted to mean that CB binds to protomers within the filament, but not to the barbed end. The reversal of activities for CH and CE, combined with the activity profile of CB, constitute the strongest evidence to date that there is more than one cytochalasin binding site on the actin molecule.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
181-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Actin filament capping and cleaving activity of cytochalasins B, D, E, and H.
pubmed:affiliation
Department of Chemistry, Syracuse University, New York 13244.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, Non-P.H.S.