Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
34
|
pubmed:dateCreated |
1992-1-13
|
pubmed:abstractText |
Metal chelate affinity chromatography has been used to follow reconstitution of the 66- and 51-kDa human immunodeficiency (HIV)-1 and HIV-2 reverse transcriptase (RT) subunits into heterodimer, as well as chimeric enzymes comprised of heterologous subunits. By adding a small N-terminal polyhistidine extension to the 51-kDa subunit of either enzyme, reconstituted RT could be recovered from a cell lysate by chromatography on Ni(2+)-nitrilotriacetic acid-Sepharose. Homologous RT subunits rapidly associated to form the respective heterodimers (1-p66.1-p51 and 2-p66.2-p51) when bacterial lysates containing the individual components were mixed. Under the same conditions, association of p66 HIV-2 and p51 HIV-1 RT was inefficient and could be improved slightly by prolonged incubation of the respective p66 and p51 subunits. In contrast, HIV-1 p66 RT rapidly associated with the 51-kDa subunit of the HIV-2 enzyme. RNA-dependent DNA polymerase activity was associated with all reconstituted enzymes, and the response of each chimeric RT to an inhibitor selective for the HIV-1 enzyme indicated that sensitivity to inhibition was determined by the source of its 66-kDa subunit.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/HIV Reverse Transcriptase,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Directed DNA Polymerase,
http://linkedlifedata.com/resource/pubmed/chemical/Reverse Transcriptase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/reverse transcriptase, Human...
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
5
|
pubmed:volume |
266
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
23003-9
|
pubmed:dateRevised |
2008-11-21
|
pubmed:meshHeading |
pubmed-meshheading:1720776-Chimera,
pubmed-meshheading:1720776-Chromatography, Gel,
pubmed-meshheading:1720776-Cloning, Molecular,
pubmed-meshheading:1720776-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1720776-Escherichia coli,
pubmed-meshheading:1720776-HIV Reverse Transcriptase,
pubmed-meshheading:1720776-HIV-1,
pubmed-meshheading:1720776-HIV-2,
pubmed-meshheading:1720776-Protein Multimerization,
pubmed-meshheading:1720776-RNA-Directed DNA Polymerase,
pubmed-meshheading:1720776-Reverse Transcriptase Inhibitors
|
pubmed:year |
1991
|
pubmed:articleTitle |
Reconstitution and properties of homologous and chimeric HIV-1.HIV-2 p66.p51 reverse transcriptase.
|
pubmed:affiliation |
Division of Infectious Diseases, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|