Linked Life Data

9019273

Source:http://linkedlifedata.com/resource/pubmed/id/9019273

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1997-2-11
pubmed:abstractText
Elongation factor 1 alpha (EF-1 alpha) is an essential factor for protein synthesis in eukaryotes. Here, we demonstrated that Tetrahymena EF-1 alpha induced bundles of rabbit skeletal muscle F-actin as well as Tetrahymena F-actin in vitro, although Tetrahymena and skeletal muscle actins are different in some parts of their primary structures and in the binding abilities to some actin-binding proteins. Co-sedimentation experiments showed that the binding ratio of Tetrahymena EF-1 alpha to skeletal muscle F-actin in the bundles was 1 : 1. Electron microscopic observation showed that alkaline pH or high ionic strength reduced the bundling activity of Tetrahymena EF-1 alpha to some extent, although the EF-1 alpha seemed to be able to induce bundling of the F-actin within the range of physiological condition.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
B
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0289-0003
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
371-5
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Characterization of F-actin bundling activity of Tetrahymena elongation factor 1 alpha investigated with rabbit skeletal muscle actin.
pubmed:affiliation
Institute of Biological Sciences, University of Tsukuba, Ibaraki, Japan.
pubmed:publicationType
Journal Article