Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1998-2-25
pubmed:abstractText
Renibacterium salmoninarum, the agent of bacterial kidney disease in salmonids, releases high concentrations of extracellular protein in tissues of infected fish. The extracellular protein consists almost entirely of a 57-kDa protein and derivatives of degradation and aggregation of the same molecule. The 57-kDa protein and its derivatives were fractionated into defined ranges of molecular mass. Separated fractions continued to produce degradation and aggregation products. One-dimensional electrophoretic separation of extracellular protein revealed a number of proteolytically active bands from > 100 to approximately 18 kDa associated with various 57-kDa protein derivatives in the different molecular mass fractions. Two-dimensional separation of extracellular protein showed that continued degradation and aggregation, similar both in location and behavior to some of the 57-kDa protein derivatives, was also displayed by the proteolytically active bands after their separation. Effects of reducing agents and sulfhydryl group proteinase inhibitors indicated a common mechanism for the proteolytically active polypeptides characteristic of a thiol proteinase. The results suggested that the 57-kDa protein and some of its derivatives undergo autolytic cleavage, releasing a proteolytically active polypeptide(s) of at least 18 kDa. Soluble polysaccharide-like material also was detected in extracellular products and tissue from infected fish. Antiserum to the polysaccharide-like material cross-reacted with O-polysaccharide of the fish pathogen Aeromonas salmonicida, suggesting some structural similarity between these polysaccharides. The polysaccharide and the proteolytic activity associated with the 57-kDa protein derivatives should be investigated with respect to the pathogenesis of R. salmoninarum infections.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-1777853, http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-1981894, http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-1987079, http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-2222123, http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-2323542, http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-2380689, http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-2482922, http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-2580026, http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-2653212, http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-3364716, http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-3524440, http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-4696702, http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/9480644-7845226
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0099-2240
pubmed:author
pubmed:issnType
Print
pubmed:volume
63
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3770-5
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Further characterization of Renibacterium salmoninarum extracellular products.
pubmed:affiliation
Department of Biology, University of New Brunswick, Fredericton, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't