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 inBiochimica et biophysica acta Vol. 1073; no. 3; pp. 509 - 513
Main Authors Hasan, Rashid, Ali, Asif, Ali, Rashid
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier B.V 09.04.1991
Elsevier
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ISSN0304-4165
0006-3002
1872-8006
DOI10.1016/0304-4165(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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ISSN:0304-4165
0006-3002
1872-8006
DOI:10.1016/0304-4165(91)90223-4