By John N. Abelson, Melvin I. Simon, Alan J. Barrett (eds)
During this quantity of tools in Enzymology and its significant other quantity 244, the chapters on particular equipment, enzymes, and inhibitors are equipped in the rational framework of the hot structures for classificationand nomenclature. a large choice of specificities of peptide bond hydrolysis are represented in each one set of peptidases, including an both wide selection of organic capabilities. Key beneficial properties* Aspartic peptidases* Metallopeptidases* New details on class of proteolytic enzymes* scientific implications of study during this sector* Biotechnological makes use of of those enzymes
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Additional resources for Proteolytic Enzymes: Aspartic and Metallo Peptidases
WISEMAN, MICHAEL GREEN, and JuDD BERMAN Introduction The optimization of substrate design is an initial step toward the development of robust enzyme assays. In addition, the information gained from the optimization procedure can serve as a basis for inhibitor design. We previously reported a method which allows rapid optimization of substrates by screening pools of specific peptide mixtures. 1 Optimal substrates can be directly identified in each pool by using a combined high-performance liquid chromatography/mass spectrometry (HPLC/MS) technique.
E. Danley, L. G. , and G. C. Andrews, FEBS Lett. 262, 119 (1990). 45 N. M. Green, Biochem. f. 90, 564 (1964). 46 A. J. Barrett, C. G. Knight, M. A. Brown, and U. Tisljar, Biochem. f. 260, 259 (1989). S. Stack and R. D. Gray, f. Bioi. Chern. 264, 4277 (1989). 42  FLUORIMETRIC ASSAYS OF PROTEOLYTIC ENZYMES 29 valuable tools in studies of the matrix metalloproteinases, 48 A 9 there are disadvantages to the use of tryptophan as a fluorophore. 2. Tryptophan is also abundant in proteins, so that assays made with crude enzyme preparations, or with protein inhibitors, will be less sensitive owing to a high fluorescence background.
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