1997
DOI: 10.1002/art.1780400724
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Correlation of serum IgG antibodies to recombinant P0 fusion protein with IgG antibodies to carboxyl‐terminal 22 synthetic peptides and carboxyl‐terminal 22 amino acid‐deleted recombinant P0 fusion protein in patients with systemic lupus erythematosus

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Cited by 3 publications
(4 citation statements)
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“…Currently, a debate is open as to whether highly purified synthetic ribosomal P peptides alone are able to adhere to plastic plates [46][47][48][49] and consequently whether recombinant fusion proteins are better than synthetic peptides as coating antigens. Our data further support the idea that attention has to be paid to the choice of the coating antigen.…”
Section: Discussionmentioning
confidence: 99%
“…Currently, a debate is open as to whether highly purified synthetic ribosomal P peptides alone are able to adhere to plastic plates [46][47][48][49] and consequently whether recombinant fusion proteins are better than synthetic peptides as coating antigens. Our data further support the idea that attention has to be paid to the choice of the coating antigen.…”
Section: Discussionmentioning
confidence: 99%
“…To confirm the presence of antibodies for the epitopes representing regions of the ribosomal P proteins other than the C-terminal 22-amino acid sequence, antibodies to recombinant ribosomal P0 protein lacking the C-terminal 22 amino acids (C22-depleted rP0) [ 21 ] were evaluated. The results clearly demonstrate that CSF anti-C22-depleted rP0 levels were significantly correlated with CSF anti-P EX.C22 levels.…”
Section: Discussionmentioning
confidence: 99%
“…Antibodies for the C-terminal 22-amino acid ribosomal P synthetic peptide (anti-P C22 ) in sera and CSF and those for purified whole ribosomal P proteins (anti-whole P) in CSF were determined by specific ELISA using the highly purified synthetic C-terminal 22-amino acid ribosomal P peptide conjugated to HSA as an antigen as previously described [ 5 ] and highly purified bovine ribosomal P proteins (P0, P1, and P2) (purity of more than 90%) (Arotec Diagnostics Limited, Wellington, New Zealand). Antibodies for the epitope representing regions of the ribosomal P proteins other than P C22 were similarly determined by ELISA using recombinant ribosomal P0 fusion protein lacking the C-terminal 22 amino acids (C22-depleted rP0) as previously described [ 21 ].…”
Section: Methodsmentioning
confidence: 99%
“…Previous studies have shown that the epitopes recognized by the RPP aAb are located mainly within the C-terminal sequence common to the three ribosomal P proteins [9,14]. These findings suggest that the RPP aAb could be detected with an enzyme-linked immunosorbent assay (ELISA) using only a C-terminal peptide of ribosomal P proteins [15] or a recombinant P0 fusion protein [16].…”
Section: Introductionmentioning
confidence: 92%