Comparative intermolecular cross-relaxation studies on human hemoglobin in red blood cells and bovine serum albumin in solution
Comparative intermolecular cross-relaxation studies on human hemoglobin in red blood cells and bovine serum albumin in solution
复制标题
红细胞中人血红蛋白与溶液中牛血清白蛋白分子间交叉弛豫比较研究
作者：
Era S;Sogami M;Uyesaka N;Kato K;Murakami M;Matsushima S;Kinosada Y
Intermolecular cross‐relaxation rate (CR) spectra [1/TIS(HDO) or 1/TIS(H2O)vs f2(ppm) profiles] for bovine serum albumin [BSA; molecular weight (MW), 66 kDa] solution, partially hydrolyzed BSA gel (BSA*gel) and packed human red blood cells (RBCs) with normal or unstable hemoglobin (Hb; MW, 65 kDa) were studied usingf2irradiation ranging from – 100 to 100 ppm atγH2/2π of 250 Hz. The CR spectra for BSA*gel (pD 4.01, 0.10MNaCl, 4.83 and 14.39%) exhibited different features in the off‐resonance region (below – 2.00 and above 12.0 ppm) relative to that for BSA solution (pD 7.14, 0.10MNaCl, 14.39%), indicating the association of BSA* molecules in the gel state. The CR spectrum for packed RBCs was compared with those for BSA*gel and BSA solution (14.39%) by correcting for differences in protein concentration. The corrected CR spectrum for packed normal RBCs in the off‐resonance region was similar to that for BSA solution, indicating that the physical characteristics of Hb in normal RBCs may be in a solution‐like state. Our results on normal RBCs were approximately consistent with the previously reported thermodynamic and hydrodynamic findings that Hb in RBCs and/or in concentrated solution seems to be in a suspension of hard scaled particles. Copyright © 2011 John Wiley & Sons, Ltd.
