Linked Life Data

6204444

Source:http://linkedlifedata.com/resource/pubmed/id/6204444

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1984-8-20
pubmed:abstractText
Two proteins, termed gp60 and p30, have been purified to homogeneity from bovine leukemia virus (BLV) using controlled pore glass and reverse-phase liquid chromatography (RPLC). gp60 was shown to be a glycoprotein by identification of glucosamine on the amino acid analyzer. Antiserum prepared to gp60 recognized in addition to gp60 a 52,000-Da polypeptide in some virus preparations, but did not cross-react with p30. The amino and carboxyl termini of gp60 were found to be tryptophan and arginine, respectively, and a 38-residue amino-terminal sequence of gp60 (NH2TrpArgXSerLeuSerLeuGlyAsnGlnGlnTrpMetThrAlaTyrAsnGlnGluAlaLys PheSerIleSerIleAspGlnIleLeuGluAlaHisAsnGlnSerProPhe-) was obtained. A 12-residue amino-terminal sequence for p30 (NH2SerProValAlaAlaLeuThrLeuGlySerAlaLeu) was also obtained. The p30 sequence showed substantial homology to the transmembrane proteins of both types B and C retroviruses and also to a deduced sequence of the 3' region of the env gene of human T-cell leukemia virus. From these results and from elution behavior of these proteins on RPLC, it was concluded that gp60 and p30 are the BLV env gene-encoded surface glycoprotein and transmembrane protein, respectively.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:volume
135
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
417-27
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
The envelope proteins of bovine leukemia virus: purification and sequence analysis.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't