Jacks T J, Neucere N J, McCall E R
Int J Pept Protein Res. 1975;7(2):153-7.
The reactivity of arachin (principal storage protein of the peanut) with anti-arachin decreased after arachin was heated at certain temperatures. Infrared and circular dichroic spectra of heated and unheated samples of arachin were examined to determine whether conformational modes changed concomitantly with decreased antigenicity. Infrared absorbances of each sample at amide I, II and V bands were essentially identical; however, absorbances at amide IV and VI bands were altered in relative intensities proportionally to the temperatures of treatment. Conformational modes, determined by circular dichroism, gradually increased in content of unordered structure from x-helical and pleated sheet modes relative to the temperature of treatment. These observations are discussed in regard to relationships of the loss of antigenicity to conformatonal changes in heated arachin.
花生球蛋白（花生的主要储存蛋白）在特定温度下加热后，其与抗花生球蛋白的反应性降低。对加热和未加热的花生球蛋白样品进行红外光谱和圆二色光谱检测，以确定构象模式是否随抗原性降低而同步变化。每个样品在酰胺I、II和V带的红外吸光度基本相同；然而，酰胺IV和VI带的吸光度相对强度随处理温度成比例变化。通过圆二色性测定的构象模式，相对于处理温度，无序结构的含量相对于α-螺旋和褶皱片层模式逐渐增加。就加热花生球蛋白中抗原性丧失与构象变化的关系对这些观察结果进行了讨论。
