Arutiunian E E, Gonchar N A, Levchenko I Ia, Gruber I M, Nikol'skaia I I
Biokhimiia. 1991 Feb;56(2):281-8.
The behaviour of methylation and restriction enzymes of Staphylococcus aureus 6782 during their isoelectrofocusing on ampholinese was studied. It was found that the RSau 6782 isoenzyme is represented by two isoforms, RI and RII, with isoelectric points of 4.2 and 7.9, respectively. Data from isoelectrofocusing analysis suggest that RI and R II are devoid of relaxed specificity found in the original preparation. In was shown that the relaxed specificity is also inherent in the isoschisomeric enzyme, RSau3A. Isoelectrofocusing of the original preparation RSau3A, as in case with RSau 6782, allows the identification of two peaks, RI and RII, and the separation of each peak from the "trace" activity. Multiple forms of DNA-methylase of the Sau 6782 type are represented by four isoenzymes possessing acidic properties. The method allows one to single out from the total methylase pool a modifying methylase with p1 (3.9) is close to that of RSau 6782 and thus the enzyme cannot serve for correct separation of restriction and methylation enzymes of Sau 6782.
研究了金黄色葡萄球菌6782的甲基化酶和限制酶在两性电解质等电聚焦过程中的行为。发现RSau 6782同工酶由两种同工型RI和RII代表，其等电点分别为4.2和7.9。等电聚焦分析数据表明，RI和R II没有原始制剂中发现的宽松特异性。结果表明，同裂酶RSau3A也具有宽松特异性。与RSau 6782一样，原始制剂RSau3A的等电聚焦允许识别两个峰，RI和RII，并将每个峰与“痕量”活性分离。Sau 6782型DNA甲基化酶的多种形式由四种具有酸性性质的同工酶代表。该方法允许从总甲基化酶库中挑选出一种修饰甲基化酶，其pI（3.9）与RSau 6782接近，因此该酶不能用于正确分离Sau 6782的限制酶和甲基化酶。
