ABSTRACT
DNA binding proteins (DBP) are shown to be engaged in the regulatory functions of the genome. Since the accelerated epidermopoesis in psoriasis indicates changed gene activities, the examination of DBP possible could help to clarify the pathological processes. Psoriatic scales were used to elaborate the method. DBP was isolated from a protein extract by affinity chromatography with DNA-cellulose according to Alberts et al. About 3-5% of postribosomal crude protein (PCP) extract had an affinity to DNA. The separation of DBP on SDS polyacrylamide slab gels showed a characteristic spectrum of proteins with molecular weights from 12.7 to 150 X 10(3) daltons. The protein band spectrum of the concentrated DBP fraction was different from that of the crude extract. These observations show the isolated DBP to represent an own group of water soluble proteins with DNA binding abilities.
