Feldberg R S, Grossman L
Biochemistry. 1976 Jun 1;15(11):2402-8. doi: 10.1021/bi00656a024.
A DNA-binding protein specific for ultraviolet irradiated DNA has been purified extensively from human placenta. The binding preparation is free of exonuclease, polymerase, endonuclease, and N-glycosidase activity. The binding activity is salt dependent and is specific for double-stranded irradiated DNA. DNA from which the pyrimidine dimers have been monomerized by the action of photolyase (photoreactivating enzyme) remains an effective substrate for the binding protein, suggesting that the protein recognizes photoproducts other than pyrimidine dimers. This is supported by the finding that DNA irradiated under conditions which introduce only pyrimidine dimers is not a substrate for the binding protein. Examination of three of the xeroderma pigmentosum complementation groups has revealed no deficiency in this binding activity.
一种对紫外线照射的DNA具有特异性的DNA结合蛋白已从人胎盘中得到广泛纯化。该结合制剂不含核酸外切酶、聚合酶、核酸内切酶和N-糖苷酶活性。结合活性依赖于盐,且对双链照射的DNA具有特异性。经光解酶(光复活酶)作用使嘧啶二聚体单体化后的DNA仍然是结合蛋白的有效底物,这表明该蛋白识别除嘧啶二聚体以外的光产物。这一观点得到以下发现的支持:在仅产生嘧啶二聚体的条件下照射的DNA不是结合蛋白的底物。对三种着色性干皮病互补组的检测表明,这种结合活性没有缺陷。