Novel DNA-protein complex and a large DNA in SLE cryoprecipitates.

Agarose gel electrophoresis of cryoprecipitates from systemic lupus erythematosus (SLE) patients revealed the presence of a slowly migrating DNAse I-sensitive DNA species at the top of the gel. Upon deproteinization, electrophoretic migration was modified favouring the migration of a 17.5 kb DNA fragment. Mixing experiments adding human serum or plasma to a lambda phage DNA digest revealed a DNA-protein interaction shown by an accumulation of high mol. wt polynucleotide at the top of the gels, and a slowed migration of the DNA bands. No comparable effect was observed when serum albumin was added to the lambda DNA digest. Dot hybridization analysis showed preferential reactivity of the 17.5 kb DNA to human DNA, implying its human origin. Our data suggests that most of this high molecular weight DNA exists as a DNA-2 protein complex. Our mixing experiments also suggest the occurrence of an excess of free DNA antibodies. We propose that the DNA-protein association may play a role in the stabilization and immunogenicity of the nucleoprotein complex.