球状蛋白质的折叠机制。来自金黄色葡萄球菌的青霉素酶作为重折叠研究模型的适用性。
The mechanism of folding of globular proteins. Suitability of a penicillinase from Staphylococcus Aureus as a model for refolding studies.
作者信息
Robson B, Pain R H
出版信息
Biochem J. 1976 May 1;155(2):325-30. doi: 10.1042/bj1550325.
Abstract
- A homogeneous preparation of penicillinase (penicillin amido-beta-lactamhydrolase, EC 3.5.2.6) was isolated and purified from cultures of Staphylococcus aureus by a simple two-stage procedure. 2. The native protein contains 20-30% helix as determined by optical-rotatory-dispersion and circular-dichroism measurements. Some 54(+/-5)% of the 13 tyrosine residues are exposed to solvent molecules of diameter 0.44 and 0.94 nm. 3. Conditions that allow full recovery of enzymic activity and native conformation from the fully unfolded state in 4M-guanidinium chloride were defined. 4. Refolding of the protein was shown to be inhibited by intermolecular interaction, by small changes in ionization and by low concentrations (0.025 M) of phenol.
摘要
- 通过一个简单的两阶段程序，从金黄色葡萄球菌培养物中分离并纯化出了青霉素酶（青霉素酰胺-β-内酰胺水解酶，EC 3.5.2.6）的均一制剂。2. 通过旋光色散和圆二色性测量确定，天然蛋白质含有20%-30%的螺旋结构。13个酪氨酸残基中约54（±5）%暴露于直径为0.44和0.94纳米的溶剂分子中。3. 确定了在4M盐酸胍中能使酶活性和天然构象从完全展开状态完全恢复的条件。4. 研究表明，分子间相互作用、电离的微小变化以及低浓度（0.025M）的苯酚会抑制蛋白质的重折叠。
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