天然和交联蜡样芽孢杆菌569/Hβ-内酰胺酶I的热变性
Thermal denaturation of native and cross-linked Bacillus cereus 569/H beta-lactamase I.
作者信息
Arnold L D, Viswanatha T
出版信息
Biochim Biophys Acta. 1983 Dec 12;749(2):192-7. doi: 10.1016/0167-4838(83)90252-2.
PMID:6418209
Abstract
Thermal denaturation of native and internally cross-linked Bacillus cereus 569/H beta-lactamase I (beta-lactamhydrolase, EC 3.5.2.6) was investigated using differential scanning calorimetry. Application of temperature-scanning kinetics provided an estimate of various activation parameters for the denaturation process. Evidence is presented to indicate that subtle temperature-induced conformational changes preceding gross denaturation are sufficient to cause inactivation of the enzyme.
摘要
利用差示扫描量热法研究了天然和内部交联的蜡样芽孢杆菌569/Hβ-内酰胺酶I（β-内酰胺水解酶，EC 3.5.2.6）的热变性。温度扫描动力学的应用提供了变性过程中各种活化参数的估计值。有证据表明，在明显变性之前细微的温度诱导构象变化足以导致酶失活。
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