Linked Life Data

8407677

Source:http://linkedlifedata.com/resource/pubmed/id/8407677

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-10-26
pubmed:abstractText
Three esterases (Est-) hydrolysing alpha-naphthyl acetate: Est-E1, Est-E3 and Est-E4 produced by Salmonella enterica serovar Typhimurium, strain LT2 were separated by DEAE chromatography and gel filtration. Est-E3, the major component of this set of enzymes, clearly differed from the two other esterases by its apparent molecular weight, titration curve, substrate specificity and inactivation. Immunoglobulins raised against Est-E3 completely neutralized the activity of Est-E3 but did not react with Est-E1 or Est-E4; it showed no cross reaction with carboxylesterase B of Escherichia coli or with carboxylesterases from other enterobacteria. Est-E3 showed electrophoretic variants which were biochemically and immunologically detected in the seven subspecies of the genus Salmonella. These findings suggest that variants of Est-E3 are the products of very closely related loci originating from a common ancestral gene. The esterase could be a phylogenetic marker of the genus and a suitable molecular tool for taxonomy and epidemiology.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-8847
pubmed:author
pubmed:issnType
Print
pubmed:volume
75
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
176-83
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Isolation and characterization of carboxylesterase E3 from Salmonella enterica.
pubmed:affiliation
Laboratoire de Microbiologie, Faculté de Médecine X. Bichat, Université Paris 7, France.
pubmed:publicationType
Journal Article