来自大鼠肝脏细胞核的脱氧核糖核酸连接酶。纯化及特性
A deoxyribonucleic acid ligase from nuclei of rat liver. Purification and properties.
作者信息
Zimmerman S B, Levin C J
出版信息
J Biol Chem. 1975 Jan 10;250(1):149-55.
A DNA ligase has been extensively purified from nuclei of rat livers. The ligase seals single strand nicks in DNA with any of the four usual bases on either the 3 or 5 sides. It requires ATP and a divalent cation (Mg-2plus or Mn-2plus) for activity. At low Mg-2plus concentrations the activity is greatly stimulated by a variety of monovalent cations. Relatively small excesses of either monovalent or divalent cation above the amounts which give maximal activity lead to inhibition of activity. Poly(G) and poly(I) inhibit ligase activity; several other polyribonucleotides are not inhibitory. Low concentrations of inorganic pyrophosphate are inhibitory. The molecular weight of the ligase is estimated from gel filtration to be about 10 times 10-4.
已从大鼠肝脏细胞核中大量纯化出一种DNA连接酶。该连接酶可封闭DNA单链切口，切口两侧的四种常见碱基中的任何一种均可，且3'或5'端均可。其活性需要ATP和二价阳离子（Mg²⁺或Mn²⁺）。在低Mg²⁺浓度下，多种单价阳离子可极大地刺激其活性。单价或二价阳离子的量略高于产生最大活性所需的量时，会导致活性受到抑制。聚鸟苷酸（Poly(G)）和聚肌苷酸（Poly(I)）可抑制连接酶活性；其他几种多聚核糖核苷酸则无抑制作用。低浓度的无机焦磷酸具有抑制作用。通过凝胶过滤估计，该连接酶的分子量约为10×10⁴。
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