Antibodies against DNA-psoralen crosslink recognize unique conformation
The DNA-psoralen crosslink induced precipitating antibodies in rabbits with a titer of 1:102400 by direct binding ELISA. The antiserum showed considerable binding with Z-DNA and calf thymus DNA brominated under high salt concentration which has been shown to attain Z-/analogous conformation. Inhibit...
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Published in | Biochimica et biophysica acta Vol. 1073; no. 3; pp. 509 - 513 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Amsterdam
Elsevier B.V
09.04.1991
Elsevier |
Subjects | |
Online Access | Get full text |
ISSN | 0304-4165 0006-3002 1872-8006 |
DOI | 10.1016/0304-4165(91)90223-4 |
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Summary: | The DNA-psoralen crosslink induced precipitating antibodies in rabbits with a titer of 1:102400 by direct binding ELISA. The antiserum showed considerable binding with Z-DNA and calf thymus DNA brominated under high salt concentration which has been shown to attain Z-/analogous conformation. Inhibition experiments substantiated the results of direct binding assay. However, the affinity purified IgG showed high degree of specificity for the immunogen and did not recognize nDNA, Z-DNA and brominated DNA as inhibitor. Poly(dG · dC) · poly(dG · dC)-psoralen photoadduct was found to be inhibitory. These results indicate that the antibodies are probably recognizing the unique conformation at the site of psoralen crosslinking. The DNA-psoralen crosslink showed significant binding with SLE sera known to have high levels of anti-native DNA antibodies. Affinity purified SLE-IgG in a competition assay pointed out the autoantibody recognition of altered conformation of DNA-psoralen crosslink. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0304-4165 0006-3002 1872-8006 |
DOI: | 10.1016/0304-4165(91)90223-4 |