单体B27赖氨酸去条纹肽胰岛素：半合成、表征及生物活性

Monomeric B27 Lys destripeptide insulin: semisynthesis, characterization and biological activity.

作者信息

Ding Jin-Guo, Cui Da-Fu, Zhang You-Shang

机构信息

Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, the Chinese Academy of Sciences, Shanghai 200031, China.

出版信息

Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2003 Mar;35(3):215-8.

PMID:12621544

Abstract

In this paper, we report the semisynthesis of B27 Lys destripeptide insulin (B27 Lys DTrI), i.e. destetrapeptide insulin with an additional Lys residue at the C-terminus of B-chain. B27 Lys DTrI is also monomeric as shown by gel filtration. Its in vivo biological activity is 80% in comparison with that of native insulin. The addition of a Lys residue at the C-terminus of B-chain makes it possible to obtain monomeric B27 Lys DTrI from a precursor expressed in Saccharomyces cerevesiae by tryptic hydrolysis instead of the less efficient tryptic transpeptidation.

摘要

在本文中，我们报道了B27赖氨酸去条带肽胰岛素（B27 Lys DTrI）的半合成，即B链C端带有一个额外赖氨酸残基的去四肽胰岛素。凝胶过滤显示B27 Lys DTrI也是单体。与天然胰岛素相比，其体内生物活性为80%。在B链C端添加一个赖氨酸残基，使得通过胰蛋白酶水解从酿酒酵母中表达的前体获得单体B27 Lys DTrI成为可能，而不是效率较低的胰蛋白酶转肽作用。