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来自单峰骆驼(骆驼属单峰驼)的血红蛋白中多阴离子诱导的构象变化。氯离子的作用。

Conformational changes induced by polyanions in haemoglobin from the dromedary (Camelus dromedarius). Role of chloride ions.

作者信息

Santucci R, Amiconi G, Ascoli F, Brunori M

出版信息

Biochem J. 1986 Dec 1;240(2):613-6. doi: 10.1042/bj2400613.

Abstract

The role of chloride ions in modulating polyanion-induced conformational changes in haemoglobin from the dromedary (Camelus dromedarius) has been investigated. The results obtained have shown that: in the ferric derivative at pH 6.5 the effect of single polyanion (dextran sulphate and inositol hexakisphosphate) on the conformation is essentially local, thus involving only the tertiary structure of the protein; the presence of chloride ions at a concentration close to the physiological value (i.e. 150 mM) is essential to induce quaternary conformational changes in the polyanion-ferric protein system; comparison between structural and functional data correlates polyanion-induced tertiary conformational changes with changes in the value of midpoint potential, E'0, and quaternary changes with co-operativity.

摘要

研究了氯离子在调节单峰驼(骆驼属单峰驼)血红蛋白中多聚阴离子诱导的构象变化方面的作用。所得结果表明:在pH 6.5的高铁衍生物中,单一多聚阴离子(硫酸葡聚糖和肌醇六磷酸)对构象的影响基本上是局部的,因此仅涉及蛋白质的三级结构;浓度接近生理值(即150 mM)的氯离子的存在对于在多聚阴离子 - 高铁蛋白系统中诱导四级构象变化至关重要;结构和功能数据之间的比较将多聚阴离子诱导的三级构象变化与中点电位E'0值的变化相关联,以及将四级变化与协同性相关联。

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Evidence for two oxygen-linked binding sites for polyanions in dromedary hemoglobin.
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本文引用的文献

5
Evidence for two oxygen-linked binding sites for polyanions in dromedary hemoglobin.
Eur J Biochem. 1985 Jul 15;150(2):387-93. doi: 10.1111/j.1432-1033.1985.tb09032.x.

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