Thomas T L, Patel G L
Biochemistry. 1976 Apr 6;15(7):1481-9. doi: 10.1021/bi00652a019.
A subclass of nonhistone chromatin proteins with high DNA affinity has been isolated from rat liver. The interaction of the isolated proteins with DNA in vitro was characterized utilizing a nitrocellulose filter binding technique. The temperature, time, concentration, ionic strength, and pH dependence were characterized. Optimal interaction was observed at 0.19 M naCl, pH 7.5 with a protein to DNA ratio of 13 (w/w). Equilibrium and kinetic competition experiments indicated that these proteins interact optimally with A-T rich and single-stranded DNA. The data also suggest that these proteins might affect the helixcoil transiton of DNA.
已从大鼠肝脏中分离出一类对DNA具有高亲和力的非组蛋白染色质蛋白。利用硝酸纤维素滤膜结合技术对分离出的蛋白质与DNA在体外的相互作用进行了表征。对温度、时间、浓度、离子强度和pH依赖性进行了表征。在0.19M氯化钠、pH 7.5、蛋白质与DNA比例为13（w/w）时观察到最佳相互作用。平衡和动力学竞争实验表明，这些蛋白质与富含A-T的DNA和单链DNA的相互作用最佳。数据还表明，这些蛋白质可能会影响DNA的螺旋-卷曲转变。
