Linked Life Data

8519066

Source:http://linkedlifedata.com/resource/pubmed/id/8519066

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-7-27
pubmed:abstractText
Isolated skeletons from human erythrocyte ghosts were studied using immunogold labeling; negative staining; and quick-freeze, deep-etch, rotary replication with Pt/C (QFDERR). Isolated skeletons visualized by QFDERR were similar to the negatively stained skeletons in that the proteins spectrin, actin, and ankyrin could be easily distinguished. However, the quick-frozen skeletons had two fewer filaments (4.2 +/- 0.7) at an actin junction. Immunogold labeling of skeletons with site-specific spectrin antibodies not only confirmed the designation of these filaments as spectrin molecules, but indicated that about 30% of spectrin filaments form non-actin junctions consistent with the hexameric organization of these filaments. Many of the filaments displayed a striking banding pattern indicative of underlying substructure. Isolated skeletons prepared by QFDERR also showed evidence of laterally associated spectrin filaments. These associations, as well as many hexamer junctions, are lost during negative staining. Negative staining also apparently caused approximately 21% of the spectrin filaments to separate into their monomeric subunits. These results indicate that the surface tension imposed during negative staining of isolated skeletons can cause a loss of interactions normally present in the intact membrane skeleton.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0886-1544
pubmed:author
pubmed:issnType
Print
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
30-42
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Ultrastructure and immunocytochemistry of the isolated human erythrocyte membrane skeleton.
pubmed:affiliation
Department of Physiology, School of Medicine, University of Maryland, Baltimore.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.