蜡样芽孢杆菌569/H/9胞外β-内酰胺酶I的构象变化
Conformational changes in the extracellular beta-lactamase I from Bacillus cereus 569/H/9.
作者信息
Davies R B, Abraham E P
出版信息
Biochem J. 1974 Oct;143(1):137-41. doi: 10.1042/bj1430137.
Abstract
- The thermal denaturation and precipitation of beta-lactamase I from Bacillus cereus 569/H/9 at 60 degrees C are reversible, a soluble and almost fully active enzyme being obtained after solution of the precipitate in 5m-guanidinium chloride or 8m-urea and subsequent removal of the denaturing agent. 2. Inactivation of beta-lactamase I occurs rapidly between 50 degrees and 55 degrees C and is shown by circular-dichroism spectra to be accompanied by an extensive conformational change. 3. A change to a different conformation occurs in 6m-urea. This change is also reversible; refolding with almost complete recovery of enzymic activity occurs within 5min of dilution of the denaturing agent. 4. Inactivation of beta-lactamase I at pH3.0 and 11.0 is also associated with conformational changes, since a proportion of the lost activity is recovered within 5min of adjustment of the pH to 7.0.
摘要
- 蜡样芽孢杆菌569/H/9中的β-内酰胺酶I在60℃下的热变性和沉淀是可逆的，将沉淀溶解于5M的氯化胍或8M的尿素中，随后去除变性剂后可得到一种可溶且几乎完全有活性的酶。2. β-内酰胺酶I在50℃至55℃之间迅速失活，圆二色光谱显示这伴随着广泛的构象变化。3. 在6M尿素中会发生向不同构象的转变。这种变化也是可逆的；在稀释变性剂后5分钟内，重新折叠并几乎完全恢复酶活性。4. β-内酰胺酶I在pH3.0和11.0时的失活也与构象变化有关，因为在将pH值调至7.0后5分钟内，一部分丧失的活性得以恢复。
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