Jacqueline Jollès, Juan Jauregui-Adell, Ida Bernier, Pierre Jollès
{"title":"La structure chimique du lysozyme de blanc d'oeuf de poule: étude détaillée","authors":"Jacqueline Jollès, Juan Jauregui-Adell, Ida Bernier, Pierre Jollès","doi":"10.1016/0006-3002(63)91033-3","DOIUrl":null,"url":null,"abstract":"<div><p>All the details concerning the establishment of the formula of the chemical structure of hen's egg-white lysozyme (<em>N</em>-acetylmuramide glycanohydrolase, EC 3.2.1.17) (which the authors had briefly indicated in 1961) are reported in the present study. The 18 tryptic units obtained from reduced lysozyme by chromatography on Dowex-1 X2 have beeb joined in the right order thanks to the chymotryptic units containing a basic amino acid and in two instances thanks to the peptic units. The protein is formed by a single polypeptide chain of 129 amino acid residues folded by the 4 bridges of the cystine residues; one of them has already been determined. Some considerations are made on the relations existing between chemical structure and biological activity.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91033-3","citationCount":"216","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et biophysica acta","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0006300263910333","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 216
Abstract
All the details concerning the establishment of the formula of the chemical structure of hen's egg-white lysozyme (N-acetylmuramide glycanohydrolase, EC 3.2.1.17) (which the authors had briefly indicated in 1961) are reported in the present study. The 18 tryptic units obtained from reduced lysozyme by chromatography on Dowex-1 X2 have beeb joined in the right order thanks to the chymotryptic units containing a basic amino acid and in two instances thanks to the peptic units. The protein is formed by a single polypeptide chain of 129 amino acid residues folded by the 4 bridges of the cystine residues; one of them has already been determined. Some considerations are made on the relations existing between chemical structure and biological activity.