Byers D M, Verpoorte J A
Biochim Biophys Acta. 1978 Apr 26;533(2):478-86. doi: 10.1016/0005-2795(78)90393-8.
The effects of guanidine hydrochloride and high temperature on human glycophorin and sialic acid-free glycophorin were monitored by circular dichroism, viscosity, and fluorescence of 1-anilino-8-naphthalane sulfonate (ANS). The following observations were made: 1. Glycophorin and its sialic acid-free counterpart are unusually stable to both guanidine . HCl and heat. 2. CD and viscosity measurements indicate that guanidine . HCl neither causes a cooperative unfolding nor generates a random coil. 3. The ANS binding site is much more sensitive to guanidine . HCl than the ellipticity at 220 nm (theta 220). 4. The effect of temperature on CD is reversible whereas the effect of guanidine . HCl is not. 5. The carbohydrate moiety influences the viscosity, and also contributes to the changes in theta 220 when solutions of glycophorin are heated. These unusual properties indicate a complex mechanism of unfolding for this structurally stable macromolecule.
通过圆二色性、粘度以及1-苯胺基-8-萘磺酸盐（ANS）荧光法监测盐酸胍和高温对人血型糖蛋白及去唾液酸血型糖蛋白的影响。得到以下观察结果：1. 血型糖蛋白及其去唾液酸对应物对盐酸胍和热均异常稳定。2. 圆二色性和粘度测量表明，盐酸胍既不会引起协同解折叠，也不会产生无规卷曲。3. ANS结合位点对盐酸胍的敏感性远高于220nm处的椭圆率（θ220）。4. 温度对圆二色性的影响是可逆的，而盐酸胍的影响则不可逆。5. 碳水化合物部分会影响粘度，并且在加热血型糖蛋白溶液时也会导致θ220的变化。这些异常特性表明这种结构稳定的大分子存在复杂的解折叠机制。
