Linked Life Data

152647

Source:http://linkedlifedata.com/resource/pubmed/id/152647

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1979-2-12
pubmed:abstractText
Actin and spectrin were isolated from washed red blood cell membranes. Spectrin bound and polymerized erythrocyte actin in the absence of potassium. Spectrin coated into polystyrene latex particles bound 8--9 mol of erythrocyte actin per mol of spectrin when actin was in its depolymerized state. Spectrin enhanced the interaction of erythrocyte actin with muscle myosin as manifested by changes in Mg2+-ATPase activity. A similar enhancement also was observed with muscle alpha-actinin while muscle tropomyosin abolished these effects. The data suggest that spectrin may play the role of polymerizing factor as well as the anchoring site for erythrocyte actin just as alpha-actinin is the anchoring site for actin filaments in muscle and other non-muscle cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
513
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
205-20
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
Erythrocyte actin and spectrin. Interactions with muscle contractile and regulatory proteins.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.