ALLFREY V, MIRSKY A E
J Gen Physiol. 1952 Nov;36(2):227-41. doi: 10.1085/jgp.36.2.227.
It has been found that many animal tissues contain "acid" desoxyribonucleases with pH optima near 5.2. A chemical method for the determination of this activity is described. The pancreatic desoxyribonuclease crystallized by Kunitz and shown to have a neutral pH optimum occurs in the pancreas together with the "acid" enzyme, but only the "neutral" enzyme occurs in the pancreatic juice. The ratio of "neutral" to "acid" DNAase activities in the pancreas is greater than 200, but in all other tissues examined there is no appreciable concentration of the neutral enzyme. It is concluded that neutral DNAase, like trypsin or lipase, has a digestive function. Some problems in the activation of the secretory enzyme in neutral pancreatic extracts are described. This activation can be interpreted in terms of a specific inhibitor or an inactive form of the enzyme. A comparison of the "acid" DNAase activities of different organs of the calf, horse, chicken, mouse, and rat indicates a possible connection between the DNAase concentration of a tissue and its capacity for proliferation or regeneration. However, the comparative DNAase activities of fetal and adult tissues do not support the view that DNAase function is limited to some simple role in the mechanics of cell division. Studies on the incorporation of glycine-N(15) into the desoxypentose nucleic acids of avian red cells, and mouse liver, pancreas, and kidney show that the N(15) uptake into the DNA of the chromosome is most rapid in tissues with high DNAase concentrations. No N(15) incorporation is observed in the DNA of avian red cells, which have negligible concentrations of the enzyme. The analyses of tissues and nuclei isolated in non-aqueous media show that the bulk of the enzyme occurs in the cytoplasm of the cell, and that nuclear concentrations vary from tissue to tissue. A theory relating the DNAase activity of the cell to its over-all desoxypentose nucleotide metabolism is discussed. No evidence has been found for the presence of inhibitors of the "acid" DNAase in animal tissues.
已发现许多动物组织含有pH最适值接近5.2的“酸性”脱氧核糖核酸酶。本文描述了一种测定该活性的化学方法。由库尼茨结晶并显示具有中性pH最适值的胰腺脱氧核糖核酸酶与“酸性”酶一起存在于胰腺中,但只有“中性”酶存在于胰液中。胰腺中“中性”与“酸性”脱氧核糖核酸酶活性的比率大于200,但在所有其他检查的组织中,中性酶没有明显的浓度。得出的结论是,中性脱氧核糖核酸酶与胰蛋白酶或脂肪酶一样,具有消化功能。本文描述了中性胰腺提取物中分泌酶激活的一些问题。这种激活可以用特异性抑制剂或酶的无活性形式来解释。对小牛、马、鸡、小鼠和大鼠不同器官的“酸性”脱氧核糖核酸酶活性的比较表明,组织的脱氧核糖核酸酶浓度与其增殖或再生能力之间可能存在联系。然而,胎儿和成年组织的比较脱氧核糖核酸酶活性并不支持脱氧核糖核酸酶功能仅限于细胞分裂机制中某些简单作用的观点。对甘氨酸-N(15)掺入禽红细胞、小鼠肝脏、胰腺和肾脏的脱氧戊糖核酸的研究表明,在脱氧核糖核酸酶浓度高的组织中(15)N掺入染色体DNA的速度最快。在酶浓度可忽略不计的禽红细胞DNA中未观察到(15)N掺入。在非水介质中分离的组织和细胞核的分析表明,大部分酶存在于细胞的细胞质中,并且核浓度因组织而异。本文讨论了一种将细胞的脱氧核糖核酸酶活性与其总体脱氧戊糖核苷酸代谢相关联的理论。未发现动物组织中存在“酸性”脱氧核糖核酸酶抑制剂的证据。