Linked Life Data

1801736

Source:http://linkedlifedata.com/resource/pubmed/id/1801736

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4-6
pubmed:dateCreated
1992-4-23
pubmed:abstractText
Based on a variety of independent assays, the expression of HIV (human immunodeficiency virus type 1) protease in living bacterial cells results in their loss of viability. Although the mechanism is not proven, we have observed degradation of cellular proteins in E. coli expressing large amounts of active HIV protease. In order to avoid the loss of viability, we devised an expression system in which the viral protease is fused to beta-lactamase and is rapidly secreted to the periplasmic space, thus reducing its duration in the cytosol. Furthermore, we find the periplasmic form of the protease is soluble and enzymatically is several-fold more active than enzyme recovered from intracellular aggregates. The question of whether the viral protease may be toxic to infected cells is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0232-766X
pubmed:author
pubmed:issnType
Print
pubmed:volume
50
pubmed:geneSymbol
pol
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
643-6
pubmed:dateRevised
2001-11-13
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
An E. coli expression system which detoxifies the HIV protease.
pubmed:affiliation
Central Research and Development Department, Du Pont Experimental Station, Wilmington, Delaware 19880-0328.
pubmed:publicationType
Journal Article