Orlovskaia N N, Demchenko A P, Veselovskaia L D
Ukr Biokhim Zh. 1977 Jan-Feb;49(1):15-9.
The experiments were aimed at studying conformation differences of muscle aldolase in normal rabbits and those fasting for a long time and at finding the areas of polypeptide chains affected by the changes. For this purpose the difference, temperature- and solvent-perturbation spectra of the compared proteins were examined. On the basis of the data obtained on the same amount of chromophore groups in both proteins a conclusion is drawn on a more hydrophobic surrounding of tyrosine and tryptophan residues in aldolase of the long-fasting animals. When determing the content of the tyrosine and tryptophan surface residues an increase (from 13 to 21) was found in the number of the tyrosine residues in aldolase of the long-fasting animals. An assumption is advanced on localization of the primary structure changes in the molecule sites rich in chromophore groups or those located closer to them.
这些实验旨在研究正常兔子和长期禁食兔子肌肉醛缩酶的构象差异，并找出受这些变化影响的多肽链区域。为此，检测了所比较蛋白质的差异光谱、温度扰动光谱和溶剂扰动光谱。基于两种蛋白质中相同数量发色团基团所获得的数据，得出结论：长期禁食动物的醛缩酶中酪氨酸和色氨酸残基周围的疏水性更强。在测定酪氨酸和色氨酸表面残基含量时，发现长期禁食动物醛缩酶中酪氨酸残基的数量增加了（从13个增加到21个）。有人提出一种假设，即分子中富含发色团基团的位点或与其相邻的位点发生了一级结构变化。
