Studies on methylmalonyl-CoA mutase from Propionibacterium shermanii.
Studies on methylmalonyl-CoA mutase from Propionibacterium shermanii.
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谢尔曼丙酸杆菌甲基丙二酰辅酶A变位酶的研究。
DOI：
10.1111/j.1432-1033.1974.tb03512.x
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发表时间：
1974
期刊：
影响因子：
--
通讯作者：
Horst Sund
中科院分区：
文献类型：
--
作者：
Boleslaw Zagalak;János Rétey;Horst Sund
1
来自谢氏丙酸杆菌的甲基丙二酰辅酶A已根据Wood等人在1964年描述的方法的修改进行纯化。
2
最终的水凝胶制剂在超离心中是均匀的，显示出以下流体动力学性质：8020，W= 7.25 S，D 020，w= 5.71 F。其分子量计算为124000。通过在经校准的Sephadex G-100柱上凝胶过滤，也表明了对于胡萝卜素-酶和羟钴（III）维生素A复合物的类似分子量。
3
在用盐酸胍处理时，甲基丙二酰辅酶A β解离成两条多肽链，这两条多肽链相似，但大小不同。十二烷基硫酸盐电泳表明两条多肽链的分子量分别为61000 ± 3000、3000和66000 ± 3000。
4
在过量羟钴（III）的存在下，丙氨酸甲基丙二酰辅酶A β结晶为粉红色的针状物，由无酶活性的抑制剂·蛋白质复合物组成。
1
Methylmalonyl-CoA mutase from Propionibacterium shermanii has been purified according to a modification of the method described by Wood et al. in 1964.
2
The final mutase preparation was homogeneous in the ultracentrifuge showing the following hydrodynamic properties: 8020,W= 7.25 S, D020,w= 5.71 F. Its molecular weight was calculated to be 124000. A similar molecular weight was indicated also by gel-filtration on a calibrated Sephadex G-100 column both for the mutase apo-enzyme and the hydroxycob(III)alamin · mutase complex.
3
On treatment with guanidine hydrochloride methylmalonyl-CoA mutase dissociates into two polypeptide chains, which are similar, though not identical in size. Dodecylsulphate electrophoresis indicated for the molecular weights of the two polypeptide chains 61000 7plusmn; 3000 and 66000 ± 3000, respectively.
4
In the presence of excess hydroxycob(III)alamin methylmalonyl-CoA mutase was crystallised as pink needles consisting of the enzymically inactive inhibitor · protein complex.