Papas T S, Pry T W, Schafer M P, Sonstegard R A
Cancer Res. 1977 Sep;37(9):3214-7.
Northern poke lymphosarcoma DNA polymerase was partially purified from particulate fractions banding at 1.15 to 1.16 g/ml from homogenates prepared from frozen necropsies of tumor-bearing pike. The enzyme behaves as a typical reverse transcriptase, in that it prefers ribotemplates to deoxytemplates. The isoelectric point (pl 5.5) is similar to that of avian myeloblastosis virus polymerase. The pike enzyme elutes from a phosphocellulose column at 0.22 M potassium phosphate, the same as avian myeloblastosis virus DNA polymerase. The enzyme activity is inhibited by pyran, a specific inhibitor of viral DNA polymerases. The most striking difference between the pike lymphoma polymerase and the other viral DNA polymerases tested is the low maximum temperature of 20 degrees, compared to 30 degrees for Rauscher leukemia virus polymerase and 38 degrees for avian myeloblastosis virus and Rous sarcoma virus.
从患有肿瘤的梭子鱼冷冻尸检制备的匀浆中，在密度为1.15至1.16 g/ml的颗粒组分中部分纯化了北美狗鱼淋巴肉瘤DNA聚合酶。该酶表现为典型的逆转录酶，即它更喜欢核糖模板而非脱氧模板。其等电点（pH 5.5）与禽成髓细胞瘤病毒聚合酶的等电点相似。狗鱼酶在0.22 M磷酸钾条件下从磷酸纤维素柱上洗脱，与禽成髓细胞瘤病毒DNA聚合酶相同。该酶活性受到病毒DNA聚合酶的特异性抑制剂吡喃的抑制。狗鱼淋巴瘤聚合酶与所测试的其他病毒DNA聚合酶之间最显著的差异是其较低的最高温度为20摄氏度，相比之下，劳氏肉瘤病毒聚合酶为30摄氏度，禽成髓细胞瘤病毒和劳斯肉瘤病毒为38摄氏度。
