Vukelić B, Ritonja A, Vitale L
Department of Organic Chemistry and Biochemistry, Rudjer Bosković Institute, Zagreb, Croatia.
Appl Microbiol Biotechnol. 1995 Nov;43(6):1056-60. doi: 10.1007/BF00166925.
From filtrates of an oxytetracycline-producing culture of Streptomyces rimosus a deoxyribonuclease was purified to homogeneity and determined to be a potent endo-DNase. It is a monomeric, basic protein (M(r) approximately 21,000; pI approximately 9.5) stable in a broad pH range but unstable to higher temperature. The enzyme has an absolute requirement for Mg2+ or Mn2+, and for its full activity requires free SH groups and a low-ionic-strength environment. Its N-terminal primary structure differs from that of other nucleases.
从龟裂链霉菌产生土霉素的培养物滤液中，一种脱氧核糖核酸酶被纯化至同质，并被确定为一种强效的内切脱氧核糖核酸酶。它是一种单体碱性蛋白质（相对分子质量约为21,000；等电点约为9.5），在较宽的pH范围内稳定，但对较高温度不稳定。该酶对Mg2+或Mn2+有绝对需求，其完全活性需要游离的巯基和低离子强度的环境。它的N端一级结构与其他核酸酶不同。
