Raman Spectra of Single Human Living Erythrocyte with the Effect of pH and Serum Albumin
WU Zheng-jie1, WANG Cheng2, LIN Zheng-chun3, JIAO Qing-ze4
1. Biomanufacturing Engineering Laboratory, Graduate School at Shenzhen, Tsinghua University, Shenzhen 518055, China 2.Department of Information Science and Technology, Zhongkai University of Agriculture and Engineering, Guangzhou 510225, China 3. Foshan Institute of Technological Standardization, Foshan 528000, China 4. Department of Chemical Engineering and Environment, Beijing Institute of Technology, Beijing 100081, China
Abstract:In the present work, a cell environment which mimicked the real body environment according to the concentration radio between serum albumin and hemoglobin was built, and the cell morphology, the membrane deformation capacity, and the structure of intracellular hemoglobin of single human living erythrocyte under the effect of pH and serum albumin were studied. It was found that at different suspension pH, the magnitude of variations in cell shape and membrane deformation capacity changes with the structural changes of the intracellular hemoglobin. At pH 4.14, 4.76 and 10.18, the loss of helical structure for hemoglobin, exposing of the hydrophobic amino acid in the globin chains, and changing of the combination of heme and globin, would completely destroy the stability of hemoglobin’s structure, which seriously changes RBC’s morphology and membrane deformation capacity. While at pH 6.51 and 7.80, the Raman spectra of erythrocytes are found to have no such changes, indicating that the structure of intracellular hemoglobin was not varied, thus the cell morphology and membrane deformation capacity are quite close to the normal values. At pH 5.49 and 8.76, RBC’s morphology and membrane deformation capacity have different degrees of variation, but the structure of intracellular hemoglobin has not changed, suggesting that the cell morphology and membrane deformation capacity may be reversible. The results suggest that in the suspension solution containing serum albumin, erythrocytes have better ability to regulate and control the variation of the extracellular pH. In summary, upon building an environment which contains the same concentration radio of serum albumin to hemoglobin in the blood, this work performed systematic studies on the effect of pH on human erythrocytes. It can not only help to solve the problems about the mechanism of the structural and functional changes of erythrocytes induced by environmental pH, but also elucidates the possible variation of the erythrocyte under different pathologic states. It is therefore significant for the prevention and treatment of some diseases.
吴正洁1,王 成2,林正春3,矫庆泽4 . pH协同血清白蛋白对单个活态人红细胞作用的拉曼光谱研究 [J]. 光谱学与光谱分析, 2014, 34(05): 1279-1283.
WU Zheng-jie1, WANG Cheng2, LIN Zheng-chun3, JIAO Qing-ze4 . Raman Spectra of Single Human Living Erythrocyte with the Effect of pH and Serum Albumin . SPECTROSCOPY AND SPECTRAL ANALYSIS, 2014, 34(05): 1279-1283.
[1] Kuzman D, Znidarcic T, Gros M, et al. Pflugers Arch., 2000, 440(1): 193. [2] Gedde M M, Yang E, Huestis W H. Biochim. Biophys. Acta, 1999, 1417(2): 246. [3] Gladwin M, Shapiro K, Daniel B. Curr Opinion Hematology, 2009, 16(6): 515. [4] Mazor D, Dvilansky A, Meyerstein, N. Vox Sang, 1994, 66(4): 264. [5] YAO Cheng-can, HUANG Yao-xiong, LI Xiao-kun, et al(姚成灿, 黄耀熊, 李校坤, 等). Chinese Science Bulletin(科学通报), 2003, 48(10): 1050. [6] KANG Li-li, HUANG Yao-xiong, LIU Wen-jing, et al. Biopolymers, 2008, 89(11): 951. [7] Eriksson L E. Biochimica et Biophysica Acta, 1990, 1036(3): 193. [8] Schechter A N. Blood, 2008, 112(10): 3927. [9] Huang Yaoxiong. Current Applied Physics, 2005, 5(5): 553. [10] Wu Yue, Huang Yaoxiong, Kang Li-li, et al. Biopolymers, 2010, 93(4): 348. [11] Siamwiza M N, Lord R C, Chen M C, et al. Biochemistry, 1975, 14(22): 4870. [12] Tu A T. Raman Spectroscopy in Biology: Principles and Applications. New York: Wiley, 1982. [13] Narayanan P. Essentials of Biophysics. New Delhi: New Age Publisher, 2000. [14] Carey P R. Biochemical Applications of Raman and Resonance Raman Spectroscopies. New York: Academic, 1982.