Glycosyltransferase and sulfotransferase activities in chick corneal stromal cells before and after in vitro culture

We have characterized a DNA binding protein (DBNP-B) from the thermoacidophilic archaeon Sulfolobus acidocaldarius with respect to its interaction with single and double stranded DNA. The protein in solution exists predominantly as dimer as indicated by cross linking studies. Binding of DBNP-B to etheno DNA and poly (dA) resulted in fluorescence enhancement and hyperchromicity respectively. Ethidium bromide intercalated into DNA was completely displaced by DBNP-B. DNase I digestion of dsDNA was increased at subsaturating concentration of the protein and was inhibited at higher concentrations. These results and electron microscopy indicate that the protein forms different types of novel complexes with DNA at different protein to DNA ratios.