Sitaĭlo S Z, Skripal' I G, Babichev V V
Mikrobiol Z. 1993 Nov-Dec;55(6):17-24.
Physical and chemical properties, as well as polypeptide structure of DNAse from Mycoplasma fermentans PG-18, have been determined. The enzyme in a native form exists probably as a decamere (10X34 kD) and manifests maximal activity at weak alkaline pH range. The temperature optimum of the enzyme is --37 degrees C. DNAse appears to be Mg2+-dependent and has its maximal activity at 10 mM MgCl2. EDTA completely inhibits DNAse activity. The given DNAse has been determined to cleave a phosphodiether bond in 3'-position of deoxyribose and to have both exo- and endonuclease activity, since it has hydrolized both native linear doublestranded DNA and closed-circle plasmid DNA.
已确定发酵支原体PG - 18来源的脱氧核糖核酸酶（DNAse）的物理化学性质以及多肽结构。该酶的天然形式可能以十聚体（10×34 kD）存在，在弱碱性pH范围内表现出最大活性。该酶的最适温度为37℃。DNAse似乎依赖Mg2 +，在10 mM MgCl2时具有最大活性。EDTA完全抑制DNAse活性。已确定该DNAse能切割脱氧核糖3'-位的磷酸二酯键，并且具有外切核酸酶和内切核酸酶活性，因为它能水解天然线性双链DNA和闭环质粒DNA。
