Byers D M, Verpoorte J A
Can J Biochem. 1979 Sep;57(9):1153-8. doi: 10.1139/o79-148.
The effects of alcohols on human glycophorin were monitored by circular dichroism, solvent perturbation of absorption spectra, fluorescence of 8-anilino-1-naphthalene sulfonate, and sedimentation equilibrium in the ultracentrifuge. Both ethanol and 2-chloroethanol gradually increase the alpha helix in glycophorin and its sialic acid free counterpart. The same alcohols do not cause a cooperative transition in the structure of the polypeptide chain of glycophorin. Other alcohols also increase the alpha-helix content of glycophorin. Binding of ANS to glycophorin is abolished at relatively low alcohol concentrations. Ethanol at 60% (v/v) reduces the molecular weight ratio of glycophorin and at the same time increases the exposure of tyrosine residues to solvent. These observations indicate a complex mechanism of interaction of weakly protic solvents with this stable membrane protein.
通过圆二色性、吸收光谱的溶剂扰动、8-苯胺基-1-萘磺酸盐荧光以及超速离心机中的沉降平衡来监测醇类对人血型糖蛋白的影响。乙醇和2-氯乙醇都会逐渐增加血型糖蛋白及其去唾液酸对应物中的α螺旋。相同的醇类不会导致血型糖蛋白多肽链结构发生协同转变。其他醇类也会增加血型糖蛋白的α螺旋含量。在相对较低的醇浓度下,ANS与血型糖蛋白的结合就会被消除。60%(v/v)的乙醇会降低血型糖蛋白的分子量比,同时增加酪氨酸残基对溶剂的暴露。这些观察结果表明,弱质子溶剂与这种稳定的膜蛋白相互作用的机制很复杂。