Guanidination of the Bowman-Birk soybean inhibitor: Evidence for the tryptic hydrolysis of peptide bonds involving homoarginine
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference16 articles.
1. Tryptic digestion of native and chemically modified α- lactalbumin
2. Preparation and Properties of Guanidinated Mercuripapain
3. The Reactive Site of Trypsin Inhibitors
4. Identifizierung von Lysin- und Argininresten als Hemmzentren von Proteaseinhibitoren mit Hilfe von Maleinsäureanhydrid und Butandion-(2.3)
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1. Comprehensive Analysis of Protein N-Terminome by Guanidination of Terminal Amines;Analytical Chemistry;2019-12-17
2. Guanidinated protein internal standard for immunoaffinity-liquid chromatography/tandem mass spectrometry quantitation of protein therapeutics;Rapid Communications in Mass Spectrometry;2014-05-22
3. Solid-phase N-terminal peptide enrichment study by optimizing trypsin proteolysis on homoarginine-modified proteins by mass spectrometry;Rapid Communications in Mass Spectrometry;2014-02-05
4. Chemical Modification of Saccharomycopsis fibuligera R64 α-Amylase to Improve its Stability Against Thermal, Chelator, and Proteolytic Inactivation;Applied Biochemistry and Biotechnology;2013-03-07
5. Effects of Guanidination with Trypsin, Lys-C, or Glu-C Digestion on Mass Spectrometric Signal Intensity and Protein Sequence Coverage;Bulletin of the Korean Chemical Society;2010-06-20
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