蛋白质多聚体的研究。β-半乳糖苷酶在甘油中的缔合-解离行为。
Studies on protein multimers. The association-dissociation behaviour of -galactosidase in glycerol.
作者信息
Contaxis C C, Reithel F J
出版信息
Biochem J. 1971 Sep;124(3):623-32. doi: 10.1042/bj1240623.
Abstract
- The effect of glycerol on the association-dissociation behaviour of beta-galactosidases from Escherichia coli is described. Two strains, K12 and ML308, were used as sources of enzyme. The conditions used, involving glycerol at a concentration of 90%, result in dissociation of the active 540000-dalton form to inactive structural subunits of 135000 daltons. 2. A pH-dependent process, assumed to be cyclic in mechanism, allows reassociation to an active form indistinguishable from the initial protein. 3. The apparently identical structural subunits, if produced in the presence of EDTA, were found to give rise to two electrophoretically distinguishable species. 4. Enzymes from both strains of E. coli can be distinguished electrophoretically but exhibit the same behaviour in glycerol. 5. A scheme of the association-dissociation is presented that is consistent with the behaviour observed and that has some predictive value.
摘要
- 描述了甘油对来自大肠杆菌的β-半乳糖苷酶缔合-解离行为的影响。使用了K12和ML308这两个菌株作为酶的来源。所采用的条件，包括90%浓度的甘油，会导致540000道尔顿的活性形式解离为135000道尔顿的无活性结构亚基。2. 一个依赖pH的过程，假定其机制是循环的，能使酶重新缔合为一种与初始蛋白质无法区分的活性形式。3. 如果在存在乙二胺四乙酸（EDTA）的情况下产生明显相同的结构亚基，会发现它们会产生两种电泳上可区分的种类。4. 来自大肠杆菌两个菌株的酶在电泳上可以区分，但在甘油中表现出相同的行为。5. 提出了一个缔合-解离的方案，该方案与观察到的行为一致且具有一定的预测价值。
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