Fronticelli C
J Biol Chem. 1978 Apr 10;253(7):2288-91.
The carbomonoxy derivatives of hemoglobin A and S showed a different optical activity in the Soret region of the spectrum as measured by circular dichroism. Different optical activity was also measured in the carbomonoxy derivatives of the beta subunits of hemoglobin A and S, the respective deoxy derivatives showed different circular dichroism spectra only in the presence of inositol hexaphosphate. Sedimentation velocity experiments showed that the differences in optical activity are not due to a different state of aggregation of the subunits. Modification of the tertiary structure of the beta subunits seems to be responsible for the phenomenon. Speculation based on the work of Hsu and Woody (Hsu, M.C., and Woody, R.W. (1971) J. Am. Chem. Soc. 93, 3515-3525) suggests the involvement of the beta15 tryptophan in the conformational changes produced by the beta6 Glu-Val mutation in hemoglobin S.
通过圆二色性测量发现，血红蛋白A和S的碳氧单氧化物衍生物在光谱的索雷特区域表现出不同的光学活性。在血红蛋白A和S的β亚基的碳氧单氧化物衍生物中也测量到了不同的光学活性，各自的脱氧衍生物仅在肌醇六磷酸存在的情况下表现出不同的圆二色光谱。沉降速度实验表明，光学活性的差异并非由于亚基的不同聚集状态所致。β亚基三级结构的改变似乎是造成这种现象的原因。基于许和伍迪的研究成果（许，M.C.，和伍迪，R.W.（1971年）《美国化学会志》93，3515 - 3525）进行的推测表明，β15色氨酸参与了血红蛋白S中β6谷氨酸 - 缬氨酸突变所产生的构象变化。
