## Abstract Protease cleavage site recognition motifs can be identified using protease substrate discovery methodologies, but typically exhibit nonβoptimal specificity and activity. To enable evolutionary optimization of substrate cleavage kinetics, a twoβcolor cellular library of peptide substrate
Kinetics of protease hydrolysis of extended peptide substrates: Measurement by flow-injection analysis
β Scribed by Georges L. Chong; Lawrence C. Davis; Gerald R. Reeck
- Book ID
- 102989408
- Publisher
- Elsevier Science
- Year
- 1990
- Tongue
- English
- Weight
- 545 KB
- Volume
- 186
- Category
- Article
- ISSN
- 0003-2697
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β¦ Synopsis
A flow-injection analysis (FIA) system was developed to study the enzyme-catalyzed hydrolysis of synthetic peptides, each of which contained one scissile bond. The concentrations of alpha-amino groups in reactions mixtures were determined by FIA with o-phthalaldehyde as a fluorescence reagent. The method allows a rapid, precise, and sensitive determination of kinetic constants for proteases acting on extended peptide substrates.
π SIMILAR VOLUMES
A kinetic method for the simultaneous determination of magnesium and calcium ions in solution is described. The method is based on the dissociation reactions of cryptand (2.2.2) complexes; a stopped-flow injection technique is used with spectrophotometric monitoring of the phthalein complexone compl