Kinetic detection of intermediates during the elastase‐catalyzed hydrolysis of succinyl‐trialanine‐p‐nitroanilide at subzero temperatures
- 1 August 1977
- journal article
- Published by Wiley in FEBS Letters
- Vol. 80 (1) , 182-186
- https://doi.org/10.1016/0014-5793(77)80435-3
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- Crystal structure of elastase–substrate complex at −55 °CNature, 1976
- Formation of stable crystalline enzyme–substrate intermediates at sub-zero temperaturesNature, 1976
- Practical potentiometric determinations of proton activity in hydro organic solvents at subzero temperaturesAnalytical Biochemistry, 1976
- Cryoenzymology of chymotrypsin: the detection of intermediates in the catalysis of a specific anilide substrateBiochemistry, 1976
- Protein crystallography at sub-zero temperatures: Lysozyme-substrate complexes in cooled mixed solventsJournal of Molecular Biology, 1975
- The synthesis and analytical use of a highly sensitive and convenient substrate of elastaseBiochemical Medicine, 1974
- Spectral Properties of an Oxygenated Luciferase—Flavin Intermediate Isolated by Low-Temperature ChromatographyProceedings of the National Academy of Sciences, 1973
- α-Chymotrypsin-catalyzed hydrolysis of N-acetyl-L-tryptophan p-nitrophenyl ester in dimethyl sulfoxide at subzero temperaturesBiochemistry, 1973
- Evidence for an Extended Active Center in ElastaseProceedings of the National Academy of Sciences, 1970
- Temporal Resolution of Individual Steps in an Enzymic Reaction at Low TemperatureProceedings of the National Academy of Sciences, 1970