4.5 Article Proceedings Paper

Kinetic characterization of sequencing grade modified trypsin

期刊

PROTEOMICS
卷 5, 期 9, 页码 2319-2321

出版社

WILEY
DOI: 10.1002/pmic.200401268

关键词

enzyme characterization; protein digestion; sample preparation; trypsin

资金

  1. NIMH NIH HHS [R01MH59926] Funding Source: Medline

向作者/读者索取更多资源

Prior to analysis by mass spectrometry, protein samples are often digested. Maximizing the peptide yield from digestion can increase the number of peptides detected and the confidence in protein identification. To determine the optimal conditions for digestion, the Michaelis-Menten kinetic parameters for Promega sequencing grade modified trypsin were measured over a range of temperatures and pHs. The results indicate that an increase in digestion temperature above 37 degrees C, the temperature traditionally used in digestion methods, could offer an increase in peptides detected.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.5
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据