Lo K Y, Bessman M J
J Biol Chem. 1976 Apr 25;251(8):2475-9.
The DNA polymerase induced by an antimutator T4 phage has been purified to apparent homogeneity and has been compared to the wild type polymerase. The mutant enzyme resembles the wild type in thermal stability, pH optimum, salt activation, divalent metal ion requirement, inhibition by a sulfhydryl reagent, and apparent affinity for DNA. However, the mutant enzyme differs from the wild type in its 8-fold higher 3'-exonuclease activity and in its decreased apparent affinity for deoxyribonucleoside triphosphates. Inhibition studies indicate that the exonuclease of the mutant enzyme is more vulnerable to physical and chemical modification than its wild type counterpart.
一种抗突变T4噬菌体诱导产生的DNA聚合酶已被纯化至表观均一，并与野生型聚合酶进行了比较。该突变酶在热稳定性、最适pH值、盐激活、二价金属离子需求、巯基试剂抑制以及对DNA的表观亲和力等方面与野生型相似。然而，该突变酶与野生型的不同之处在于其3'-外切核酸酶活性高8倍，且对脱氧核糖核苷三磷酸的表观亲和力降低。抑制研究表明，突变酶的外切核酸酶比其野生型对应物更容易受到物理和化学修饰的影响。
