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关于甲泛葡胺-蛋白质相互作用的研究。

Studies on metrizamide-protein interactions.

作者信息

Hüttermann A, Wendlberger-Schieweg G

出版信息

Biochim Biophys Acta. 1976 Nov 26;453(1):176-84. doi: 10.1016/0005-2795(76)90261-0.

Abstract
  1. The apparent density of catalase after isopycnic centrifugation in metrizamide gradients is dependent on the metrizamide concentration into which the enzyme is dissolved at the beginning of the centrifugation. 2. This different behaviour of the enzyme in metrizamide gradients is due to the formation of a metrizamide-protein complex which is more dense than the uncomplexed catalase. 3. A bimodal distribution of the catalase, with additional heavy bands, was only observed in metrizamide gradients in light water, where rather high metrizamide concentrations are needed even for a banding of the uncomplexed enzyme. 4. The half-life of the metrizamide-protein complex is less than 5 min. This was shown by spectroscopical measurements and band sedimentation analysis in an analytical ultracentrifuge.
摘要
  1. 在甲泛葡胺梯度中进行等密度离心后,过氧化氢酶的表观密度取决于离心开始时酶溶解于其中的甲泛葡胺浓度。2. 该酶在甲泛葡胺梯度中表现出的这种不同行为是由于形成了一种比未复合的过氧化氢酶密度更大的甲泛葡胺 - 蛋白质复合物。3. 仅在轻水中的甲泛葡胺梯度中观察到过氧化氢酶的双峰分布以及额外的重带,即使对于未复合酶的条带化,也需要相当高的甲泛葡胺浓度。4. 甲泛葡胺 - 蛋白质复合物的半衰期小于5分钟。这通过光谱测量和分析超速离心机中的条带沉降分析得以证明。

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