Back to Search
Start Over
Antigenic structure of DN A: relatively high inhibitory activity of di--and trideoxyribonudeotide derived from DNase digest on the interaction of thermally denatured DNA with systemic lupus erythematosus sera.
- Source :
-
Clinical & Experimental Immunology . Feb1981, Vol. 43 Issue 2, p223-230. 8p. - Publication Year :
- 1981
-
Abstract
- The antigenic determinant of thermally denatured DNA reactive with systemic lupus erythematosus (SLE) sera was examined by hapten inhibition assay. We used oligonucleotides with different chain lengths (2-8) derived from DNase I digests of salmon sperm DNA in Farr's radioimmunoassay with thermally denatured mouse embryo 3H-DNA as antigen, and the effect of dextran sulphate addition to the assay mixture on the inhibitory activity of oligonucleotides was examined, A characteristic oligonucleotide inhibition pattern on DNA binding by SLE sera was observed in the assay system without dextran sulphate. Di- and/or trinucleotide inhibited the binding more effectively than tetra- and/or pentanucleotide. These patterns were also observed in DNA-normal serum interaction. When dextran sulphate was added to the mixture, the inhibition pattern changed; the inhibitory activity of oligonucleotides increased with chain length in both serum groups. The inhibitory potency of di- and trinucleotide was higher on DNA-SLE sera than on DNA normal sera interaction. The high potency of short-chain oligomers in SLE sera is obviously different from that in experimentally elicited anti-DNA sera suggesting that different mechanism(s) are involved In antibody production in normal individuals and SLE patients. [ABSTRACT FROM AUTHOR]
- Subjects :
- *GENES
*NUCLEIC acids
*SERUM
*BLOOD plasma
*OLIGONUCLEOTIDES
*NUCLEOTIDES
Subjects
Details
- Language :
- English
- ISSN :
- 00099104
- Volume :
- 43
- Issue :
- 2
- Database :
- Academic Search Index
- Journal :
- Clinical & Experimental Immunology
- Publication Type :
- Academic Journal
- Accession number :
- 16011976