• 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

Carboxylesterases (EC 3.1.1). Purification and titration of chicken, sheep, and horse liver carboxylesterases.

作者信息

Inkerman P A, Scott K, Runnegar M T, Hamilton S E, Bennett E A, Zerner B

出版信息

Can J Biochem. 1975 May;53(5):536-46. doi: 10.1139/o75-074.

DOI:10.1139/o75-074
PMID:1139397
Abstract

Chicken, sheep, and horse liver carboxylesterases have been purified by procedures involving ammonium sulfate fractionation, ion-exchange chromatography and gel filtration on Sephadex. The actual yields of the procedures described were as follows: chicken, 1 g from 2 kg of liver powder (chloroform-acetone); sheep, 200 mg from 400 g of powder (chloroform-acetone); horse, 230 mg from 800 g of powder (acetone). The purified enzymes are free of non-carboxyl-esterase protein as shown by gel electrophoresis, although they do contain electrophoretic variants. The equivalent weight of the chicken enzyme is 67,000 based on titration with p-nitrophenyl diethyl phosphate or bis(p-nitrophenyl) phosphate, whereas those of the sheep and horse enzymes are similar to 69,500 and similar to 70,000, respectively, based on titration with p-nitrophenyl dimethylcarbamate.

摘要

相似文献

1
Carboxylesterases (EC 3.1.1). Purification and titration of chicken, sheep, and horse liver carboxylesterases.
Can J Biochem. 1975 May;53(5):536-46. doi: 10.1139/o75-074.
2
Carboxylesterases from chicken, sheep, and horse liver.来自鸡、绵羊和马肝脏的羧酸酯酶。
Methods Enzymol. 1975;35:208-21. doi: 10.1016/0076-6879(75)35156-2.
3
Organophosphate inhibitors: the reactions of bis(p-nitrophenyl) methyl phosphate with liver carboxylesterases and alpha-chymotrypsin.有机磷酸酯抑制剂:双(对硝基苯基)甲基磷酸酯与肝脏羧酸酯酶和α-胰凝乳蛋白酶的反应
Biochim Biophys Acta. 1975 Feb 19;377(2):282-96. doi: 10.1016/0005-2744(75)90310-1.
4
Carboxylesterases (EC 3.1.1). A comparison of some kinetic properties of horse, sheep, chicken, pig, and ox liver carboxylesterases.
Can J Biochem. 1975 May;53(5):565-73. doi: 10.1139/o75-077.
5
Carboxylesterases (EC 3.1.1). The molecular sizes of chicken and pig liver carboxylesterases.
Can J Biochem. 1975 May;53(5):547-60. doi: 10.1139/o75-075.
6
Carboxylesterases (EC 3.1.1). A large-scale purification of pig liver carboxylesterase.
Biochemistry. 1969 May;8(5):2000-6. doi: 10.1021/bi00833a033.
7
Carboxylesterases (EC 3.1.1). Purification and titration of ox liver carboxylesterase.
Biochemistry. 1969 May;8(5):2013-8. doi: 10.1021/bi00833a035.
8
Carboxylesterases (EC 3.1.1). Amino acid composition of liver carboxylesterases.羧酸酯酶(EC 3.1.1)。肝脏羧酸酯酶的氨基酸组成。
Can J Biochem. 1975 May;53(5):561-4. doi: 10.1139/o75-076.
9
[Simple and rapid methods for the preparation of highly purified carboxylesterases (EC 3.1.1.1) from porcine and bovine liver and porcine kidneys (author's transl)[].从猪和牛肝脏以及猪肾脏中制备高纯度羧酸酯酶(EC 3.1.1.1)的简单快速方法(作者译)
Hoppe Seylers Z Physiol Chem. 1974 Feb;355(2):155-63.
10
On the homology of the active-site peptides of liver carboxylesterases.关于肝脏羧酸酯酶活性位点肽段的同源性
Biochim Biophys Acta. 1969 Jan 7;171(1):128-37. doi: 10.1016/0005-2744(69)90112-0.

引用本文的文献

1
Tumour-selective targeting of drug metabolizing enzymes to treat metastatic cancer.肿瘤选择性靶向药物代谢酶以治疗转移性癌症。
Br J Pharmacol. 2016 Oct;173(19):2811-8. doi: 10.1111/bph.13553. Epub 2016 Aug 22.
2
Horse carboxylesterases: evidence for six CES1 and four families of CES genes on chromosome 3.马羧酸酯酶:3 号染色体上 6 个 CES1 和 4 个 CES 基因家族的证据。
Comp Biochem Physiol Part D Genomics Proteomics. 2009 Mar;4(1):54-65. doi: 10.1016/j.cbd.2008.10.004. Epub 2008 Nov 5.
3
The histochemistry of carboxylester hydrolases: problems and possibilities.
羧酸酯水解酶的组织化学:问题与可能性
Histochem J. 1983 Feb;15(2):111-37. doi: 10.1007/BF01042281.