Linked Life Data

2478630

Source:http://linkedlifedata.com/resource/pubmed/id/2478630

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1989-11-30
pubmed:abstractText
A bacterial outer membrane protein of 35-kDa Mr has been reported to react with several anti-HLA-B27 mAb. Here, we demonstrated that this protein showed the heat-modifiability of the OmpA protein during SDS-PAGE. Further, the protein was not detected in mutants of Escherichia coli in which the expression of the OmpA protein has been suppressed. The protein would be reexpressed when one of the mutants was transformed with an expression vector carrying the OmpA gene. Finally, the identity of the reactive protein to OmpA protein was verified by homology in amino acid sequences. An NH2-terminal fragment of this protein was generated by tryptic digestion. Inasmuch as this was unreactive with the anti-HLA-B27 antibody, we concluded that the carboxyl-terminus contributed directly or indirectly to the reactive domain.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
143
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2955-60
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
The bacterial outer membrane protein that reacts with anti-HLA-B27 antibodies is the OmpA protein.
pubmed:affiliation
Department of Medicine, University of California, Los Angeles 90024-167022.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't