{"title":"Propriétés d'un noyau cytochromique b2 résultant d'une protéolyse de la l-lactate: Cytochrome c oxydoréductase de la levure","authors":"Françoise Labeyrie , Olga Groudinsky , Yvette Jacquot-Armand , 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.