Linked Life Data

17656789

Source:http://linkedlifedata.com/resource/pubmed/id/17656789

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2007-7-27
pubmed:abstractText
Human adenovirus proteinase (AVP), the first member of a new class of cysteine proteinases, is required for the synthesis of infectious virus. As such, it is an attractive target for proteinase inhibitors that act as antiviral agents. However, before potential inhibitors can be screened, a quick, sensitive, and quantitative assay for the enzyme is required. Here, methods for purification of a recombinant AVP expressed in Escherichia coli are presented and a fluorogenic substrate is designed, synthesized, and purified and then used in the development of a quick, sensitive, and quantitative assay for the enzyme. The reporting group in the substrate is Rhodamine 110, possibly the most detectable compound known. The substrate contains the proteinase consensus cleavage sequence (Leu-Arg-Gly-Gly). The synthesis and purification of (Leu-Arg-Gly-Gly-NH)2-Rhodamine is described. It is then used to develop assays with AVP and its various cofactors. The resultant assays are quite sensitive; enzyme activity at low nanomolar concentrations can readily be detected.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1543-1894
pubmed:author
pubmed:issnType
Print
pubmed:volume
131
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
257-67
pubmed:dateRevised
2007-12-3
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Assay for the adenovirus proteinase: purification of the enzyme and synthesis of a fluorogenic substrate.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, N.I.H., Extramural