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rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
1
|
|
pubmed:dateCreated |
2002-2-7
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|
pubmed:abstractText |
We describe the use of a new baculovirus expression vector to enable the secretion of the major surface glycoprotein of HIV-1 (gp120) fused to the carboxy-terminus of the widely used affinity tag glutathione S-transferase. The secreted protein can be purified in a single step with the minimum of denaturation on immobilised glutathione and is as active as the parental molecule in binding CD4. We use this molecule in a variety of assay formats to examine the gp120 interaction with CD26, a reported auxiliary molecule in the HIV entry process. We find no evidence of a CD26-gp120 interaction in the absence or presence of CD4.
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|
pubmed:language |
eng
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|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Apr
|
|
pubmed:issn |
0042-6822
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
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|
pubmed:day |
1
|
|
pubmed:volume |
208
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
142-6
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|
pubmed:dateRevised |
2010-11-18
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|
pubmed:meshHeading |
|
|
pubmed:year |
1995
|
|
pubmed:articleTitle |
Expression and purification of glutathione S-transferase-tagged HIV-1 gp120: no evidence of an interaction with CD26.
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pubmed:affiliation |
NERC Institute of Virology, Oxford, United Kingdom.
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|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
