Jean Chevallier, Yvette Jacquot-Armand, Jeannine Yon
{"title":"Recherche d'une activité enzymatique dans les hydrolysats de trypsine","authors":"Jean Chevallier, Yvette Jacquot-Armand, Jeannine Yon","doi":"10.1016/0926-6569(64)90012-4","DOIUrl":null,"url":null,"abstract":"<div><p>Some previous studies have seemed to prove the evidence of an active peptide occurring from trypsin (EC 3.4.4.4) hydrolysate. It had been obtained either by peptic hydrolysis of acetyltrypsinogen or by tryptic autolysis.</p><p>In the present paper, the different experiments are tried again and discussed. With both methods, the enzymatic activity finally obtained is related with the presence of unhydrolysed trypsin in the active fraction. Spectral analysis of this fraction shows that an important part of the enzyme is denatured.</p></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 3","pages":"Pages 521-528"},"PeriodicalIF":0.0000,"publicationDate":"1964-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90012-4","citationCount":"2","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926656964900124","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 2
Abstract
Some previous studies have seemed to prove the evidence of an active peptide occurring from trypsin (EC 3.4.4.4) hydrolysate. It had been obtained either by peptic hydrolysis of acetyltrypsinogen or by tryptic autolysis.
In the present paper, the different experiments are tried again and discussed. With both methods, the enzymatic activity finally obtained is related with the presence of unhydrolysed trypsin in the active fraction. Spectral analysis of this fraction shows that an important part of the enzyme is denatured.