Linked Life Data

3060142

Source:http://linkedlifedata.com/resource/pubmed/id/3060142

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1989-2-7
pubmed:abstractText
In vitro 14C-prelabelled cytosol proteins from rat hepatocytes were incubated with [3H]arginyl-tRNA in ATP-Tris-Mg-KCl-dithioerithrol medium and arginyltransferase, subsequently treated with RNase A, and the double-labelled proteins were isolated by gel filtration. The affinity of these [3H]arginylated-14C-labelled cytosol proteins to hydrophobic surfaces was investigated with octyl-Sepharose, phenyl-Sepharose and with FPLC on phenyl-Superose (HR 5/5). All 3H/14C-ratios of the proteins in the column fractions show that arginylated proteins bind preferentially to the hydrophobic matrices: the fractions eluted first show low 3H/14C-ratios, and after addition of ethylene glycol and especially of Tween 80 the 3H/14C-ratios markedly increase. Furthermore, these arginylated proteins aggregate preferentially after incubation of the cytosol proteins for 2 h at 37 degrees C and are more rapidly degraded by endopeptidases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0177-3593
pubmed:author
pubmed:issnType
Print
pubmed:volume
369 Suppl
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
307-10
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Surface hydrophobicity, arginylation and degradation of cytosol proteins from rat hepatocytes.
pubmed:affiliation
Physiologisch-chemisches Institut der Universität Tübingen.
pubmed:publicationType
Journal Article