[Theoretical possibilities and limitations of protease primary specificity determination by statistical analysis of MALDI mass-spectra of proteolysis products].

Bioorganicheskaia khimiia Pub Date : 2012-01-01
M I Drachevskaia, A V Borzenkova, N L Eremeev
{"title":"[Theoretical possibilities and limitations of protease primary specificity determination by statistical analysis of MALDI mass-spectra of proteolysis products].","authors":"M I Drachevskaia,&nbsp;A V Borzenkova,&nbsp;N L Eremeev","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Possibilities and limitations of method examination of proteolytic enzymes' primary specificity by statistical analysis of MALDI (matrix-assisted laser desorption/ionization) mass spectra of products obtained by protein substrates proteolysis without direct determination of their amino acid sequences were investigated theoretically. The optimum ranges given by the errors of the peptides masses measuring for the fabrication of statistical set of the events and the form of statistical data presentation were chosen. It was shown that the proposed method can be applied only for proteases with a relatively narrow primary specificity (two or three amino acids). The influence of protein substrate molecular weight and amino acid composition on the efficiency of specific to a particular protease amino acids display under statistical treatment of the set of proteolysis products masses was studied on the model of trypsin, chymotrypsin, glutamylendopeptidase, pepsin (pH 1.3).</p>","PeriodicalId":9325,"journal":{"name":"Bioorganicheskaia khimiia","volume":"38 1","pages":"111-8"},"PeriodicalIF":0.0000,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Bioorganicheskaia khimiia","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

Abstract

Possibilities and limitations of method examination of proteolytic enzymes' primary specificity by statistical analysis of MALDI (matrix-assisted laser desorption/ionization) mass spectra of products obtained by protein substrates proteolysis without direct determination of their amino acid sequences were investigated theoretically. The optimum ranges given by the errors of the peptides masses measuring for the fabrication of statistical set of the events and the form of statistical data presentation were chosen. It was shown that the proposed method can be applied only for proteases with a relatively narrow primary specificity (two or three amino acids). The influence of protein substrate molecular weight and amino acid composition on the efficiency of specific to a particular protease amino acids display under statistical treatment of the set of proteolysis products masses was studied on the model of trypsin, chymotrypsin, glutamylendopeptidase, pepsin (pH 1.3).

[蛋白水解产物MALDI质谱统计分析确定蛋白酶一级特异性的理论可能性和局限性]。
本文从理论上探讨了在不直接测定蛋白质底物蛋白水解产物氨基酸序列的情况下,通过基质辅助激光解吸/电离(MALDI)质谱统计分析方法检测蛋白质水解酶主要特异性的可能性和局限性。选择了肽质量测量误差给出的最佳范围,用于事件统计集的制作和统计数据的表示形式。结果表明,该方法仅适用于初级特异性较窄的蛋白酶(2个或3个氨基酸)。以胰蛋白酶、糜凝胰蛋白酶、谷氨酰胺肽酶、胃蛋白酶(pH 1.3)为模型,研究了蛋白质底物分子量和氨基酸组成对统计处理下特定蛋白酶对特定氨基酸表现效率的影响。
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