论文部分内容阅读
本文报道以圆二色性方法在相同条件下测得S-硫甲基型A链的α螺旋、β折迭的含量为15％及27％;B链为22％,23％;A和B链混合后为24％,26％。表明A和B链相混后肽链构象有一定调整,α螺旋含量有所增加。以还原型A及B链进行实验,也得到类似结果。加入二巯基苏糖醇明显减少A及B链的有序成分。上述结果表明胰岛素A及B链有一定二级结构;在能重组成胰岛素的最适条件下,A及B链相混后,因次级键相互作用,两肽链构象有一定调整,有序程度有所提高。
In this paper, the α-helix of S-thiomethyl type A chain was measured under the same conditions by circular dichroism. The content of β-sheet was 15% and 27%, while that of B chain was 22% and 23% The chain was mixed 24%, 26%. It shows that the conformation of the peptide chain is changed after the A and B chains are mixed, and the α-helix content is increased. Experiments with reduced A and B chains also yielded similar results. Dithiothreitol addition significantly reduced the orderly composition of the A and B chains. The above results show that insulin A and B chain have a certain secondary structure; under the optimal conditions that can be recombined into insulin, after the A and B chains are mixed, due to the interaction of secondary bonds, the conformations of the two peptide chains are adjusted and ordered The degree has increased.