Affinity of a DNA with highly repetitive sequence for nuclear proteins from rat liver.
A nuclear scaffold fraction (designated P fraction elsewhere) comparable to a nuclear matrix was prepared from rat liver. This fraction was composed mainly of 45-49 kDa proteins and high-molecular-weight proteins (more than 90 kDa). In addition, a 370-bp repetitive sequence DNA fragment was derived predominantly from the EcoRI digest of the deproteinized P fraction. By an immunoblot affinity assay with the P fraction, the fragment was shown to have affinity for each of the 107- and 115-kDa proteins. Moreover, by a filter binding assay with a mixture of these proteins, the affinity level was estimated to be about 6 times as high in the native (double-stranded) fragment as in the denatured (single-stranded) fragment.
Asano
S
S
Cell Biology Division, Faculty of Pharmaceutical Sciences, Toyama Medical & Pharmaceutical University, Japan.
Hibino
Y
Y
Ikeda
Y
Y
Iwakami
N
N
Sugano
N
N
D000818:Animals; D004247:DNA; D015246:Deoxyribonuclease EcoRI; D015151:Immunoblotting; D008099:Liver / Q000378:metabolism*; D009687:Nuclear Proteins / Q000235:genetics*; D051381:Rats; D012091:Repetitive Sequences, Nucleic Acid
D009687:Nuclear Proteins; D004247:DNA; D015246:Deoxyribonuclease EcoRI