The isolation of a new warfarin-sensitive protein from bovine plasma.
The isolation of a new warfarin-sensitive protein from bovine plasma.
复制标题
从牛血浆中分离出一种新的华法林敏感蛋白。
DOI：
10.1042/bst0050255
复制
发表时间：
1977
影响因子：
3.9
通讯作者：
M. Esnouf
中科院分区：
文献类型：
--
作者：
C. Prowse;M. Esnouf
在30%(v/v)二恶英中固定化的硫酰胺脱氢酶。在二恶英中失活的速率常数，与90°C下热失活的速率常数一样，随着与基质距离的增加而增加，最终接近天然酶在30%(v/v)二恶英中失活的速率常数，即0.01min-‘。亲水性琼脂糖凝胶基质可能以刚性构象持有酶，因此酶离基质骨架越近，其稳定性越高，这一事实可以合理地解释这些数据。这些观察结果与Manecke(1962)报告的与疏水基质聚苯乙烯结合的蛋白质的不稳定性形成了鲜明对比。
immobilized lipoamide dehydrogenase in 30 % (v/v) dioxan. The rate constants for inactivation in dioxan, like those for thermal inactivation at 90°C, increase with increasing distance from the matrix and eventually approach that for the inactivation of the native enzyme in 30% (v/v) dioxan, i.e. 0.01 min-'. These data can be rationalized by the fact that the hydrophilic Sepharose matrix probably holds the enzyme in a rigid conformation, and thus the nearer the enzyme is to the matrix backbone, the greater its stability. These observations contrast markedly with the destabilization of proteins bound to the hydrophobic matrix polystyrene reported by Manecke (1962).