Propriétés d'un noyau cytochromique b2 résultant d'une protéolyse de la l-lactate: Cytochrome c oxydoréductase de la levure

Françoise Labeyrie , Olga Groudinsky , Yvette Jacquot-Armand , Liliane Naslin
{"title":"Propriétés d'un noyau cytochromique b2 résultant d'une protéolyse de la l-lactate: Cytochrome c oxydoréductase de la levure","authors":"Françoise Labeyrie ,&nbsp;Olga Groudinsky ,&nbsp;Yvette Jacquot-Armand ,&nbsp;Liliane Naslin","doi":"10.1016/0926-6593(66)90010-5","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The tryptic hydrolysis of cytochrome <em>b</em><sub>2</sub> (yeast <span>l</span>-lactate: cytochrome <em>c</em> oxidoreductase, EC 1.1.2.3) liberates a cytochromic polypeptide which can be separated from the other fragments by gel filtration.</p></span></li><li><span>2.</span><span><p>2. The properties of this new product, called “noyau cytochromique <em>b</em><sub>2</sub>”, have been investigated: the molecular weight is about 11 000 and this molecule is associated with one heme group; its spectral properties are very similar in the visible region to those of cytochrome <em>b</em><sub>2</sub>. The redox potential is −0.028 V to be compared with the value 0.000 V relative to cytochrome <em>b</em><sub>2</sub> (pH 7.00; 30°). Severa, different components have been detected by electrophoresis. These data have been used in a discussion on the structural aspects of the active molecule of lactate dehydrogenase.</p></span></li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 3","pages":"Pages 492-503"},"PeriodicalIF":0.0000,"publicationDate":"1966-12-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90010-5","citationCount":"52","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/0926659366900105","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 52

Abstract

  • 1.

    1. The tryptic hydrolysis of cytochrome b2 (yeast l-lactate: cytochrome c oxidoreductase, EC 1.1.2.3) liberates a cytochromic polypeptide which can be separated from the other fragments by gel filtration.

  • 2.

    2. The properties of this new product, called “noyau cytochromique b2”, have been investigated: the molecular weight is about 11 000 and this molecule is associated with one heme group; its spectral properties are very similar in the visible region to those of cytochrome b2. The redox potential is −0.028 V to be compared with the value 0.000 V relative to cytochrome b2 (pH 7.00; 30°). Severa, different components have been detected by electrophoresis. These data have been used in a discussion on the structural aspects of the active molecule of lactate dehydrogenase.

l-乳酸蛋白水解产生的细胞色素b2核的性质:酵母细胞色素c氧化还原酶
1.1. 细胞色素b2(酵母l-乳酸:细胞色素c氧化还原酶,EC 1.1.2.3)的胰蛋白酶水解可释放一种细胞色素多肽,该多肽可通过凝胶过滤与其他片段分离。该新产物被称为“noyau cytochromique b2”,其性质已被研究:该分子的分子量约为11000,与一个血红素基团相关;它的光谱性质在可见区与细胞色素b2非常相似。氧化还原电位为- 0.028 V,相对于细胞色素b2 (pH 7.00;30°)。通过电泳检测出几种不同的成分。这些数据已用于乳酸脱氢酶活性分子的结构方面的讨论。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
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