单峰驼血红蛋白中多阴离子诱导的构象变化。对氧衍生物的圆二色性研究。
Conformational changes induced by polyanions in haemoglobin from Camelus dromedarius. Circular-dichroism study on the oxy derivative.
作者信息
Santucci R, Ascoli F, Amiconi G, Bertollini A, Brunori M
出版信息
Biochem J. 1985 Nov 1;231(3):793-6. doi: 10.1042/bj2310793.
Abstract
The c.d. spectrum of oxyhaemoglobin from Camelus dromedarius is significantly affected by the presence of inositol hexakisphosphate. Correlation with O2-binding measurements shows that these dichroic changes parallel the functional properties of the protein. The optical modifications suggest that, in contrast with human haemoglobin, the conformational changes induced by inositol hexakisphosphate on dromedary oxyhaemoglobin are mainly attributable to a local change of the tertiary structure reminiscent of that of the deoxy derivative, the quaternary conformation seeming to be almost unaffected. The results provide direct evidence of the existence on the protein of two distinct sites for polyanions.
摘要
来自单峰骆驼的氧合血红蛋白的圆二色光谱受肌醇六磷酸的存在显著影响。与氧气结合测量的相关性表明，这些二色性变化与蛋白质的功能特性平行。光学修饰表明，与人类血红蛋白不同，肌醇六磷酸在单峰骆驼氧合血红蛋白上诱导的构象变化主要归因于三级结构的局部变化，类似于脱氧衍生物的变化，四级构象似乎几乎未受影响。结果为蛋白质上存在两个不同的多阴离子结合位点提供了直接证据。
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引用本文的文献
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Conformational changes induced by polyanions in haemoglobin from Camelus dromedarius. Studies on the ferric derivatives.多聚阴离子诱导单峰驼血红蛋白的构象变化。对三价铁衍生物的研究。
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2
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