D-氨基酸氧化酶中拟议的温度依赖性构象转变：差示扫描量热法研究
Proposed temperature-dependent conformational transition in D-amino acid oxidase: a differential scanning microcalorimetric study.
作者信息
Sturtevant J M, Mateo P L
出版信息
Proc Natl Acad Sci U S A. 1978 Jun;75(6):2584-7. doi: 10.1073/pnas.75.6.2584.
Abstract
A number of authors have reported observations on D-amino acid oxidase [D-amino acid: O2 oxidoreductase (deaminating), EC 1.4.3.3.] that they have interpreted in terms of a temperature-dependent conformational transition having a van't Hoff enthalpy amounting to more than 1 cal per g of protein (1 cal = 4.184J). No indication of this transition is obtained by using a differential scanning calorimeter having a sensitivity considerably in excess of that required to detect such a transition. The implications of this discrepancy are discussed.
摘要
许多作者报告了关于D-氨基酸氧化酶[D-氨基酸：O2氧化还原酶（脱氨基），EC 1.4.3.3.]的观察结果，他们将其解释为温度依赖性构象转变，其范特霍夫焓超过每克蛋白质1卡（1卡 = 4.184焦耳）。使用灵敏度远高于检测这种转变所需灵敏度的差示扫描量热计，未获得这种转变的迹象。讨论了这种差异的影响。
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