蜡样芽孢杆菌磷脂酶C在氯化胍溶液中的去折叠与重折叠
Unfolding and refolding of phospholipase C from Bacillus cereus in solutions of guanidinium chloride.
作者信息
Little C, Johansen S
出版信息
Biochem J. 1979 Jun 1;179(3):509-14. doi: 10.1042/bj1790509.
Abstract
- Protein-fluorescence studies indicated that phospholipase C from Bacillus cereus is denatured in solutions of guanidinium chloride. The denaturation was not thermodynamically reversible and followed biphasic kinetics. 2. Guanidinium chloride solutions released the structural Zn2+ from the enzyme and rendered all histidine residues chemically reactive. In the presence of free Zn1+ the enzyme was much more resistant to denaturation. Also, the addition for free Zn2+ to the denatured enzyme induced refolding. 3. The Zn2+-free apoenzyme was much more sensitive to guanidinium chloride than was the native enzyme and the denaturation appeared to be thermodynamically reversible. 4. Guanidinium chloride denaturation was associated with a reversible inactivation of the enzyme. Heat-inactivated, coagulated enzyme was substantially re-activated on dissolution in guanidinium chloride solutions followed by dialysis against a Zn2+-containing buffer.
摘要
- 蛋白质荧光研究表明，蜡样芽孢杆菌的磷脂酶C在氯化胍溶液中会变性。这种变性在热力学上是不可逆的，并且遵循双相动力学。2. 氯化胍溶液会从该酶中释放出结构锌离子，并使所有组氨酸残基具有化学反应活性。在有游离锌离子存在的情况下，该酶对变性的抵抗力更强。此外，向变性酶中添加游离锌离子会诱导其复性。3. 不含锌离子的脱辅基酶比天然酶对氯化胍更为敏感，并且这种变性在热力学上似乎是可逆的。4. 氯化胍变性与该酶的可逆失活有关。热失活、凝固的酶在溶解于氯化胍溶液中，然后用含锌离子的缓冲液进行透析后，会大量重新激活。
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