Banerjee R K
Eur J Biochem. 1979 Jun;97(1):59-64. doi: 10.1111/j.1432-1033.1979.tb13085.x.
An adenosine triphosphatase (ATPase EC 3.6.1.3) was partially purified from myeloblasts of chicken infected with the avian myeloblastosis virus and some of its molecular, catalytic and immunological properties were compared with that of the ATPase purified from the virus. Both the enzymes possessed almost same electrophoretic mobility, molecular weight, S20,w value, substrate specificity, metal-ion requirement, apparent Km value and sensitivity to inhibitors and activator. Evidence also indicated immunological identity of the two enzymes. The insensitivity of this enzyme to rutamycin or ouabain and extreme sensitivity to most of the detergents, trypsin and mercurials are the remarkable properties of this enzyme.
从感染禽成髓细胞瘤病毒的鸡成髓细胞中部分纯化出一种三磷酸腺苷酶（ATP酶，EC 3.6.1.3），并将其一些分子、催化和免疫学特性与从该病毒中纯化出的ATP酶进行了比较。两种酶具有几乎相同的电泳迁移率、分子量、S20,w值、底物特异性、金属离子需求、表观Km值以及对抑制剂和激活剂的敏感性。证据还表明这两种酶具有免疫学同一性。该酶对鱼藤酮或哇巴因不敏感，而对大多数去污剂、胰蛋白酶和汞剂极度敏感，这些是该酶的显著特性。
