Linked Life Data

2546760

Source:http://linkedlifedata.com/resource/pubmed/id/2546760

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1989-9-1
pubmed:abstractText
Human rhinovirus type 14 protease 3C was expressed as a soluble and active protein in Escherichia coli. The protease was purified by a cationic-exchange step followed by gel filtration on a TSK 3000 column. The final yield of purified protease was in the range 0.5-1.0 mg/l culture grown to A550 = 1.0. Sequence analysis revealed that greater than 90% of the N-terminal residues were methionine. The enzyme activity of the purified protease was measured by cleavage of a synthetic peptide representing a predicted Gln/Gly viral polyprotein cleavage site. A mutant protease (Cys146----Ser) was produced and purified in the same way. The yield of mutant protease 3C was approximately 150 micrograms/l from a culture grown to A550 = 1.0. This mutant protease 3C did not cleave the synthetic peptide substrate.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
182
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
547-55
pubmed:dateRevised
2007-10-11
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
The expression and purification of human rhinovirus protease 3C.
pubmed:affiliation
Genetics Department, Glaxo Group Research, Greenford, Middlesex, England.
pubmed:publicationType
Journal Article