大鼠肝脏半胱氨酸磺酸形成酶系统的特点

Lena Ewetz, Bo Sörbo
{"title":"大鼠肝脏半胱氨酸磺酸形成酶系统的特点","authors":"Lena Ewetz,&nbsp;Bo Sörbo","doi":"10.1016/0926-6593(66)90176-7","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The oxidation of cysteine to cysteinesulfinate by rat-liver preparations in the presence of hydroxylamine has been studied. This compound is added to the assay system in order to inhibit the enzymatic destruction of the reaction product.</p></span></li><li><span>2.</span><span><p>2. The optimum assay conditions for the enzyme system are reported.</p></span></li><li><span>3.</span><span><p>3. The reaction is catalysed by a heat-labile factor found in the soluble fraction and is stimulated by TPNH, ferrous ions and mitochondria or microsomes. The stimulating activity in the particulate fractions is heat-labile.</p></span></li><li><span>4.</span><span><p>4. The enzyme system appears to be specific for <span>l</span>-cysteine, as very little sulfinate formation was detected when <span>d</span>-cysteine, <span>l</span>-cystine, glutathione or cysteamine was used as substrate.</p></span></li><li><span>5.</span><span><p>5. Among different rat tissues studied, only liver contained significant activity.</p></span></li><li><span>6.</span><span><p>6. The enzyme system is inhibited by heavy-metal reagents (EDTA, cyanide, <em>o</em>-phenanthroline) and by the sulfhydryl reagents <em>p</em>-hydroxymercuribenzoate and iodoacetate, but not by arsenite.</p></span></li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1966-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90176-7","citationCount":"68","resultStr":"{\"title\":\"Characteristics of the cysteinesulfinate-forming enzyme system in rat liver\",\"authors\":\"Lena Ewetz,&nbsp;Bo Sörbo\",\"doi\":\"10.1016/0926-6593(66)90176-7\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>1. The oxidation of cysteine to cysteinesulfinate by rat-liver preparations in the presence of hydroxylamine has been studied. This compound is added to the assay system in order to inhibit the enzymatic destruction of the reaction product.</p></span></li><li><span>2.</span><span><p>2. The optimum assay conditions for the enzyme system are reported.</p></span></li><li><span>3.</span><span><p>3. The reaction is catalysed by a heat-labile factor found in the soluble fraction and is stimulated by TPNH, ferrous ions and mitochondria or microsomes. The stimulating activity in the particulate fractions is heat-labile.</p></span></li><li><span>4.</span><span><p>4. The enzyme system appears to be specific for <span>l</span>-cysteine, as very little sulfinate formation was detected when <span>d</span>-cysteine, <span>l</span>-cystine, glutathione or cysteamine was used as substrate.</p></span></li><li><span>5.</span><span><p>5. Among different rat tissues studied, only liver contained significant activity.</p></span></li><li><span>6.</span><span><p>6. The enzyme system is inhibited by heavy-metal reagents (EDTA, cyanide, <em>o</em>-phenanthroline) and by the sulfhydryl reagents <em>p</em>-hydroxymercuribenzoate and iodoacetate, but not by arsenite.</p></span></li></ul></div>\",\"PeriodicalId\":100160,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1966-11-15\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6593(66)90176-7\",\"citationCount\":\"68\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0926659366901767\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926659366901767","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 68

摘要

1.1. 研究了在羟胺存在下,大鼠肝制剂将半胱氨酸氧化成半胱氨酸磺酸盐。这种化合物被添加到测定系统中是为了抑制酶对反应产物的破坏。报道了该酶体系的最佳测定条件。该反应由可溶性组分中的热不稳定因子催化,并由TPNH、铁离子和线粒体或微粒体刺激。颗粒组分中的刺激活性是热不稳定的。该酶系统似乎对l-半胱氨酸具有特异性,因为当d-半胱氨酸、l-半胱氨酸、谷胱甘肽或半胱氨酸作为底物时,很少检测到亚硫酸盐的形成。在研究的不同大鼠组织中,只有肝脏具有显著活性。该酶体系受重金属试剂(EDTA、氰化物、邻菲罗啉)和巯基试剂对羟基汞苯甲酸酯和碘乙酸酯的抑制,但不受亚砷酸盐的抑制。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Characteristics of the cysteinesulfinate-forming enzyme system in rat liver

  • 1.

    1. The oxidation of cysteine to cysteinesulfinate by rat-liver preparations in the presence of hydroxylamine has been studied. This compound is added to the assay system in order to inhibit the enzymatic destruction of the reaction product.

  • 2.

    2. The optimum assay conditions for the enzyme system are reported.

  • 3.

    3. The reaction is catalysed by a heat-labile factor found in the soluble fraction and is stimulated by TPNH, ferrous ions and mitochondria or microsomes. The stimulating activity in the particulate fractions is heat-labile.

  • 4.

    4. The enzyme system appears to be specific for l-cysteine, as very little sulfinate formation was detected when d-cysteine, l-cystine, glutathione or cysteamine was used as substrate.

  • 5.

    5. Among different rat tissues studied, only liver contained significant activity.

  • 6.

    6. The enzyme system is inhibited by heavy-metal reagents (EDTA, cyanide, o-phenanthroline) and by the sulfhydryl reagents p-hydroxymercuribenzoate and iodoacetate, but not by arsenite.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信