Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1988-8-19
pubmed:abstractText
We have purified a 10,774-dalton protein from human immunodeficiency virus (HIV) type 1 that is encoded in the protease domain of the pol open reading frame (ORF). Radiochemical amino acid microsequencing identified 12 amino acids from the stretch of 39 N-terminal residues of this protein, beginning with a PQITLW sequence at position 69 of the pol ORF. Radiosequencing of selected tryptic peptides of the protein identified 11 additional residues (Leu-9 and Val-2) in six peptides encompassing the entire molecule of 99 residues. A protein of similar size and identical N-terminal sequence (determined through the first 39 residues) was present among the processed HIV pol gene products in Escherichia coli which expressed the entire HIV pol ORF. The C terminus of both the viral and E. coli-expressed proteins was inferred to be contiguous with the N terminus of the p64-p51 reverse transcriptase on the basis of tryptic mapping and specific immunoreactivity with an antiserum against a dodecapeptide located upstream of the reverse transcriptase. Thus, the initial processing of the pol precursor that generates the native protease is apparently preserved across phylogenetic barriers. Although the purified viral protease lacked measurable proteolytic activity, the bacterial extracts were capable of processing an HIV gag precursor protein synthesized in E. coli.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-212597, http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-2416054, http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-2418504, http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-2419593, http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-2430111, http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-2433465, http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-2436298, http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-2444031, http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-2447506, http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-2984774, http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-2997990, http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-3005629, http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-3016298, http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-3035577, http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-3321060, http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-3882995, http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-3885215, http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-3925005, http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-6160263, http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-6343759, http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-78989, http://linkedlifedata.com/resource/pubmed/commentcorrection/3292793-90424
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-538X
pubmed:author
pubmed:issnType
Print
pubmed:volume
62
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3053-8
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Purification and structural characterization of the putative gag-pol protease of human immunodeficiency virus.
pubmed:affiliation
Laboratory of Molecular Microbiology, Program Resources, Inc., Frederick Cancer Research Facility, Maryland 21701.
pubmed:publicationType
Journal Article