Refraction, fluorescence, and Raman spectroscopy of normal and glycated hemoglobin E. N. Lazareva, A. Y. Zyubin, I. G. Samusev [et al.]
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ArticleContent type: Текст Media type: электронный Subject(s): преломление | показатель преломления | приращение температуры | флуоресценция | рамановская спектроскопия | гемоглобин | гликированный гемоглобинGenre/Form: статьи в журналах Online resources: Click here to access online
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Proceedings of SPIE Vol. 10685 : Biophotonics: Photonic solutions for better health care VI. P. 1068540-1-1068540-8Abstract: In this study, the optical properties of glycated (HbA1c) and non-glycated (Hb) hemoglobin are compared using refractometry, fluorescence and Raman spectroscopy. The fluorescence measured at an excitation wavelength of 270 nm indicates differences in the molecular structure of hemoglobins. Analysis of the spectral shift of Raman spectra also showed variations indicating differences in their molecular structure. The refractive index measured in the visible and near IR regions for different temperatures allowed for quantification of mean values of temperature increment, which are quite different as dn/dT= –(1.03 ± 0.05)×10–4 °C–1 for Hb and – (1.37 ± 0.07)×10–4 °C–1for HbA1c.The data obtained in the work can serve as a basis for further study of the optical properties of glycated hemoglobin and other glycated proteins.
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In this study, the optical properties of glycated (HbA1c) and non-glycated (Hb) hemoglobin are compared using refractometry, fluorescence and Raman spectroscopy. The fluorescence measured at an excitation wavelength of 270 nm indicates differences in the molecular structure of hemoglobins. Analysis of the spectral shift of Raman spectra also showed variations indicating differences in their molecular structure. The refractive index measured in the visible and near IR regions for different temperatures allowed for quantification of mean values of temperature increment, which are quite different as dn/dT= –(1.03 ± 0.05)×10–4 °C–1 for Hb and – (1.37 ± 0.07)×10–4 °C–1for HbA1c.The data obtained in the work can serve as a basis for further study of the optical properties of glycated hemoglobin and other glycated proteins.
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