• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

牛生长激素中羧基末端二硫键的选择性还原与烷基化

Selective reduction and alkylation of the COOH-terminal disulfide bridge in bovine growth hormone.

作者信息

Gráf L, Li C H, Bewley T A

出版信息

Int J Pept Protein Res. 1975;7(6):467-73. doi: 10.1111/j.1399-3011.1975.tb02467.x.

DOI:10.1111/j.1399-3011.1975.tb02467.x
PMID:1238375
Abstract

Conditions leading to the cleavage of both disulfide bridges in human growth hormone caused the reduction of only one disulfide bond in bovine growth hormone. Partially reduced and alkylated derivatives of bovine growth hormone were prepared and characterized. It was shown that the reduction and alkylation modified the COOH-terminal disulfide bond, however, this modification does not result in the dissociation of the dimeric form of bovine growth hormone or cause a significant loss of growth-promoting activity.

摘要

导致人生长激素中两个二硫键断裂的条件只会使牛生长激素中的一个二硫键还原。制备并表征了牛生长激素的部分还原和烷基化衍生物。结果表明,还原和烷基化修饰了羧基末端的二硫键,然而,这种修饰并不会导致牛生长激素二聚体形式的解离,也不会导致促生长活性的显著丧失。

相似文献

1
Selective reduction and alkylation of the COOH-terminal disulfide bridge in bovine growth hormone.牛生长激素中羧基末端二硫键的选择性还原与烷基化
Int J Pept Protein Res. 1975;7(6):467-73. doi: 10.1111/j.1399-3011.1975.tb02467.x.
2
Studies on prolactin. Selective reduction of the disulfide bonds of the ovine hormone.催乳素研究。绵羊激素中二硫键的选择性还原。
Biochemistry. 1979 Oct 30;18(22):4851-60. doi: 10.1021/bi00589a013.
3
Dissociation of bovine seminal ribonuclease into catalytically active monomers by selective reduction and alkylation of the intersubunit disulfide bridges.
Biochemistry. 1975 Mar 25;14(6):1116-22. doi: 10.1021/bi00677a004.
4
Optical activity of disulfide bonds in proteins. 1. Studies on plasmin modified human somatotropin.蛋白质中二硫键的旋光性。1. 对纤溶酶修饰的人生长激素的研究。
Biochemistry. 1977 Jan 25;16(2):209-15. doi: 10.1021/bi00621a008.
5
Studies on the disulfide bonds of glycoprotein hormones. Formation and properties of 11,35-bis(S-alkyl) derivatives of the alpha subunit.糖蛋白激素二硫键的研究。α亚基11,35-双(S-烷基)衍生物的形成与性质。
J Biol Chem. 1979 Feb 25;254(4):1164-9.
6
Optical activity of disulfide bonds in proteins: studies on human choriomammotropin and bovine pituitary somatotropin.蛋白质中二硫键的旋光性:关于人绒毛膜促乳腺素和牛垂体生长激素的研究
Biochemistry. 1977 Oct 4;16(20):4408-14. doi: 10.1021/bi00639a013.
7
Recombinant hormones from fragments of human growth hormone and human placental lactogen.来自人生长激素和人胎盘催乳素片段的重组激素。
J Biol Chem. 1981 Jan 10;256(1):296-300.
8
Disulfide exchange folding of insulin-like growth factor I.胰岛素样生长因子I的二硫键交换折叠
Biochemistry. 1992 Feb 18;31(6):1749-56. doi: 10.1021/bi00121a024.
9
Studies on pituitary prolactin. 39. Reaction of the ovine hormone with hydrogen peroxide.垂体催乳素研究。39. 绵羊激素与过氧化氢的反应。
Biochim Biophys Acta. 1976 Jul 19;439(1):240-9. doi: 10.1016/0005-2795(76)90179-3.
10
Action of thrombin on ovine, bovine and human pituitary growth hormones.凝血酶对绵羊、牛和人垂体生长激素的作用。
Eur J Biochem. 1976 May 1;64(2):333-40. doi: 10.1111/j.1432-1033.1976.tb10306.x.

引用本文的文献

1
Extraordinarily stable disulfide-linked homodimer of human growth hormone.人生长激素异常稳定的二硫键连接的同型二聚体。
Protein Sci. 2005 Apr;14(4):902-13. doi: 10.1110/ps.041048805. Epub 2005 Mar 1.
2
Structural characterization of the two refold dimers of recombinant bovine somatotropin (bST).重组牛生长激素(bST)两种重折叠二聚体的结构表征
J Protein Chem. 1993 Apr;12(2):237-45. doi: 10.1007/BF01026046.
3
Covalent cross-linking of the bovine somatotropin dimer. Effects on growth-promoting, receptor-binding and immunological activities and preliminary characterization of the self-association.
牛生长激素二聚体的共价交联。对生长促进、受体结合及免疫活性的影响以及自缔合的初步表征。
Biochem J. 1983 Jan 1;209(1):107-15. doi: 10.1042/bj2090107.