• 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

Partial purification of human renin substrate.

作者信息

Schioler V, Damkjaer M, Nielsen M, Kappelgaard A M, Giese J

出版信息

Eur J Clin Invest. 1976 Jun 21;6(3):229-40. doi: 10.1111/j.1365-2362.1976.tb00515.x.

DOI:10.1111/j.1365-2362.1976.tb00515.x
PMID:939246
Abstract

A two-step purification method is described for the preparation of renin substrate from human plasma. Pooled plasma from women on oral contraceptives is used for the purification. The overall yield of renin substrate is 57%, with a twenty-fold purification. The specific renin substrate content of the preparation, as determined by enzymatic degradation with an excess of human renin, is 2 mug angiotensin I per mg protein. The product has a very low endogenous renin activity and is free from angiotensinase activity. An additional purification step involving affinity chromatography is described. In pilot studies a renin substrate yield of 37% has been achieved, with a hundred-fold purification. The final product has a specific renin substrate content of 10 mug angiotensin I per mg protein. The preparation contains up to 12 different plasma proteins, nine of which have been identified and quantitated.

摘要

相似文献

1
Partial purification of human renin substrate.
Eur J Clin Invest. 1976 Jun 21;6(3):229-40. doi: 10.1111/j.1365-2362.1976.tb00515.x.
2
Purification and partial characterization of human angiotensinogen.
Biochim Biophys Acta. 1976 Mar 18;427(1):208-17. doi: 10.1016/0005-2795(76)90297-x.
3
Purification, properties and kinetics of sheep and human renin substrates.绵羊和人肾素底物的纯化、性质及动力学
Aust J Exp Biol Med Sci. 1975 Feb;53(1):77-88. doi: 10.1038/icb.1975.8.
4
Human angiotensinogen. Purification partial characterization, and a comparison with animal prohormones.
J Biol Chem. 1977 Mar 10;252(5):1654-62.
5
Separation of human renin substrate from renin and a major contaminating albumin using a concanavalin A-sepharose column.
Clin Chim Acta. 1977 Feb 1;74(3):203-6. doi: 10.1016/0009-8981(77)90286-8.
6
Evidence against inhibition of the renin-angiotensinogen reaction by des-angiotensin substrate in the rat.
Clin Sci Mol Med Suppl. 1976 Dec;3:155s-157s. doi: 10.1042/cs051155s.
7
Partial purification of dog angiotensinogen.犬血管紧张素原的部分纯化
Am J Physiol. 1979 Jun;236(6):E655-9. doi: 10.1152/ajpendo.1979.236.6.E655.
8
Purification of human angiotensinogen.人血管紧张素原的纯化
Circ Res. 1977 Oct;41(4 Suppl 2):29-33. doi: 10.1161/01.res.41.4.29.
9
Isolation of human angiotensinogen.
Biochim Biophys Acta. 1976 Sep 28;446(1):87-95. doi: 10.1016/0005-2795(76)90100-8.
10
Simultaneous measurement of renin and renin substrate concentration in human plasma by a simple kinetic method.
Clin Chim Acta. 1976 Dec;73(3):475-9. doi: 10.1016/0009-8981(76)90150-9.

引用本文的文献

1
Central role for sodium in the pathogenesis of blood pressure changes independent of angiotensin, aldosterone and catecholamines in type 1 (insulin-dependent) diabetes mellitus.钠在1型(胰岛素依赖型)糖尿病血压变化发病机制中起核心作用,该作用独立于血管紧张素、醛固酮和儿茶酚胺。
Diabetologia. 1987 Aug;30(8):610-7. doi: 10.1007/BF00277316.
2
Effect of captopril on kidney function in insulin-dependent diabetic patients with nephropathy.卡托普利对胰岛素依赖型糖尿病肾病患者肾功能的影响。
Br Med J (Clin Res Ed). 1986 Aug 23;293(6545):467-70. doi: 10.1136/bmj.293.6545.467.
3
Effect of captopril on blood pressure and kidney function in normotensive insulin dependent diabetics with nephropathy.
卡托普利对血压正常的胰岛素依赖型糖尿病肾病患者血压及肾功能的影响。
BMJ. 1989 Aug 26;299(6698):533-6. doi: 10.1136/bmj.299.6698.533.
4
Human plasma angiotensinogen: a review of purification procedures.人血浆血管紧张素原:纯化方法综述。
Mol Cell Biochem. 1979 Sep 28;27(1):47-56. doi: 10.1007/BF00849278.