Abstract
A fraction of low mobility group (LMG) nonhistone protein designated LMG 160 was isolated from rat liver chromatin by preparative gel electrophoresis and its interaction with DNA was studied using thermal denaturation and DNA–cellulose affinity chromatography techniques. The results showed that LMG 160 with an isoelecteric point of 5–5.5 was bound to DNA and decreased its melting temperature. Increasing ionic strengths decreased this effect. DNA–cellulose affinity chromatography showed the affinity of LMG 160 to double stranded DNA was higher than that to single stranded DNA, since it required 0.6 M NaCl for elution. The results suggest that LMG 160 protein preferentially binds to double stranded DNA destabilizes it and the binding is electrostatic.
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