Recherche d'une activité enzymatique dans les hydrolysats de trypsine

Jean Chevallier, Yvette Jacquot-Armand, Jeannine Yon
{"title":"Recherche d'une activité enzymatique dans les hydrolysats de trypsine","authors":"Jean Chevallier,&nbsp;Yvette Jacquot-Armand,&nbsp;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.

胰蛋白酶水解物酶活性的研究
先前的一些研究似乎已经证明了胰蛋白酶(EC 3.4.4.4)水解产物中存在活性肽的证据。它可以通过乙酰胰蛋白酶原的消化酶水解或胰蛋白酶自溶得到。本文对不同的实验进行了重新尝试和讨论。通过这两种方法,最终获得的酶活性与活性部分中未水解胰蛋白酶的存在有关。光谱分析表明,酶的一个重要部分是变性的。
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