Chernov A V, Zheleznaia L A, Matvienko N I
Biokhimiia. 1995 Aug;60(8):1318-25.
A site-specific endonuclease capable of recognizing the sequence 5'-AAGCTT-3' was detected and purified to homogeneity from the thermophilic strain of Bacillus species KT8. The endonuclease has a molecular mass of 34 kDa and is found in solution in a monomeric form. The activity of BspKT8 does not depend on ATP and is not stimulated by S-adenosyl-L-methionine. The enzyme displays the highest activity with a broad range of temperatures (37 degrees-48 degrees C). Since DNA cleavage occurs in accordance with the scheme: [formula: see text] the enzyme can be assigned to the class-II of restriction endonucleases and represents an isoschizomer of HindIII.
从嗜热芽孢杆菌属KT8菌株中检测到一种能够识别序列5'-AAGCTT-3'的位点特异性内切核酸酶,并将其纯化至同质。该内切核酸酶的分子量为34 kDa,以单体形式存在于溶液中。BspKT8的活性不依赖于ATP,也不受S-腺苷-L-甲硫氨酸的刺激。该酶在广泛的温度范围(37℃-48℃)内表现出最高活性。由于DNA切割按照以下模式发生:[公式:见文本],该酶可归为II类限制性内切核酸酶,是HindIII的同裂酶。