Linked Life Data

2220070

Source:http://linkedlifedata.com/resource/pubmed/id/2220070

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1990-11-9
pubmed:abstractText
The protein and glycoprotein composition of a sucrose gradient fraction from vaccinia infected cells treated with rifampicin was studied. This particulate fraction contained cytoplasmic membranes and pleomorphic membranous structures. The glycoproteins (89, 42 and 20-23 kDa, respectively) were identified as the same glycoproteins that are found in plasma membranes of infected cells and the envelope of extracellular enveloped vaccinia (EEV). These glycoproteins could be solubilized by 0.1% NP-40. The Golgi membrane associated 41K acylated vaccinia protein was also NP-40 soluble. In contrast, most particulate fraction proteins (125, 100, 86, 65, 41, 39, 31, 27, 25, 14 and 12.5 kDa) with the exception of the 33 and 29 kDa proteins remained essentially insoluble after NP-40 treatment. The 86 and 65 kDa proteins are the rifampicin inhibited precursors to INV core proteins while the 33 and 29 kDa proteins are INV surface proteins. Twelve proteins behaved like their respective comigrating INV proteins when extracted with NP-40 and 2ME. Electron microscopy showed that a centrifuged sediment from NP-40 treated cells contained pleomorphic protein containing membranous structures that we have called rifampicin bodies. We conclude that (1) the major glycoproteins found in the particulate fraction from sucrose gradients are vaccinia glycoproteins residing in cytoplasmic membranes while (2) the major non-glycosylated proteins are components of the rifampicin bodies and that (3) the rifampicin bodies represent an intermediate in the morphogenetic process leading to mature INV.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0168-1702
pubmed:author
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15-30
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
The polypeptide composition of vaccinia-infected cell membranes and rifampicin bodies.
pubmed:affiliation
Department of Virology, Karolinska Institute, School of Medicine SBL, Stockholm, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't