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去五肽(B26 - 30)胰岛素的结构研究。I. 去五肽胰岛素的制备与性质

Structural studies on des-pentapeptide (B26-30)-insulin. I. The preparation and properties of des-pentapeptide-insulin.

出版信息

Sci Sin. 1976 May-Jun;19(3):351-7.

PMID:788152
Abstract

It has been suggested in our previous reports that the B-chain C-terminal peptide sequence of the insulin molecule plays an important role in the primary biological activity of this hormone. It is interesting, therefore, to study the structure-function relationship of a series of related insulin analogues. An improved method has been used in this paper for the preparation of des-pentapeptide (B26-30)-insulin (DPI) suitable for the growth of single crystals. These crystals possess 88% of the receptor binding activity of insulin and exhibit hormonal activity of 20 I.U. per milligramme in the mouse convulsion test. In the presence of zinc ions, DPI cross-reacts immunologically with insulin antibody.

摘要

我们之前的报告表明,胰岛素分子的B链C末端肽序列在该激素的主要生物活性中起重要作用。因此,研究一系列相关胰岛素类似物的结构-功能关系很有意思。本文采用了一种改进的方法来制备适用于单晶生长的去五肽(B26 - 30)胰岛素(DPI)。这些晶体具有胰岛素88%的受体结合活性,并且在小鼠惊厥试验中表现出每毫克20国际单位的激素活性。在锌离子存在的情况下,DPI与胰岛素抗体发生免疫交叉反应。

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