Brockes J P
Biochem J. 1973 Aug;133(4):629-33. doi: 10.1042/bj1330629.
The bacteriophage P1 modification enzyme was purified 1400-fold from induced lysogens of a thermoinducible mutant of bacteriophage P1. The most purified fraction, when analysed by polyacrylamide-gel electrophoresis in sodium dodecyl sulphate, showed two principal stained bands. The two bands co-sedimented in a glycerol gradient with the modification activity, at a rate which, when compared with the rate of sedimentation of marker proteins, corresponds to a sedimentation coefficient in water of 6S. The mobilities of the bands on sodium dodecyl sulphate-polyacrylamide-gel electrophoresis corresponded to polypeptides of molecular weight 70000 and 45000 and they were present in equimolar amounts. It was concluded that the 6S species of the enzyme is a dimer of unlike subunits.
从噬菌体P1的热诱导突变体的诱导溶源菌中纯化出噬菌体P1修饰酶，纯化倍数达1400倍。经十二烷基硫酸钠聚丙烯酰胺凝胶电泳分析，最纯的级分显示出两条主要的染色带。这两条带在甘油梯度中与修饰活性一起共沉降，与标记蛋白的沉降速率相比，其沉降速率相当于在水中的沉降系数为6S。在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳上，这两条带的迁移率对应于分子量为70000和45000的多肽，且它们以等摩尔量存在。得出的结论是，该酶的6S种类是由不同亚基组成的二聚体。
