Francalanci F, Davis N K, Fuller J Q, Murfitt D, Leadlay P F
Biochem J. 1986 Jun 1;236(2):489-94. doi: 10.1042/bj2360489.
5'-Deoxyadenosylcobalamin-dependent methylmalonyl-CoA mutase was purified to homogeneity from Propionibacterium shermanii by a simplified procedure. The native enzyme has an apparent Mr of 165,000, similar to the enzyme from other sources but larger than previously reported. It consists of two non-identical subunits, of Mr 79,000 and 67,000 respectively. The smaller subunit is apparently not a proteolytic fragment of the larger one. The final preparation usually contained some inactive mutase, bearing a tenaciously bound cobalamin species. This protein proved to be readily separable from apoenzyme by fast protein liquid chromatography on anion-exchange columns.
采用简化方法从谢氏丙酸杆菌中纯化出了5'-脱氧腺苷钴胺素依赖性甲基丙二酰辅酶A变位酶，并使其达到了均一状态。天然酶的表观分子量为165,000，与其他来源的酶相似，但比之前报道的要大。它由两个不同的亚基组成，分子量分别为79,000和67,000。较小的亚基显然不是较大亚基的蛋白水解片段。最终制备物通常含有一些无活性的变位酶，其带有紧密结合的钴胺素种类。通过阴离子交换柱上的快速蛋白质液相色谱法，证明该蛋白很容易与脱辅基酶蛋白分离。
