Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-3-30
pubmed:abstractText
A major cell envelope protein was purified from the cell envelope fraction of Treponema denticola ATCC 35405 by ion exchange chromatography after extraction with Zwittergent 3-14. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed a relative molecular mass of 53 kDa for this protein with a pI of 6.3-6.8. Amino acid analysis revealed that this protein contained high proportions of hydrophobic amino acids (40.4%), and no cysteine could be detected. The N-terminus of the protein was blocked to Edman degradation. Rabbit antiserum raised against the purified 53 kDa protein reacted with the outer envelope of the T. denticola cell surface as confirmed by immunoelectron microscopy. This rabbit antiserum reacted with 4 of the 11 strains of treponemes tested in this study. Sera from 9 to 18 periodontitis patients reacted strongly with this 53 kDa cell envelope protein of T. denticola as determined by immunoblotting analysis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
D
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0022-3484
pubmed:author
pubmed:issnType
Print
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
70-8
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Isolation and characterization of a 53 kDa major cell envelope protein antigen from Treponema denticola ATCC 35405.
pubmed:affiliation
Department of Oral Microbiology, Okayama University Dental School, Japan.
pubmed:publicationType
Journal Article