Kinetic Studies of the Binding of Bovine Basic Pancreatic Trypsin Inhibitor to α-Chymotrypsin

Autor:	Ulrich Quast, H. Heumann, G. Krause, Erna Steffen, Jürgen Engel
Rok vydání:	1974
Předmět:	chemistry.chemical_classification Chymotrypsin biology Kunitz STI protease inhibitor Stereochemistry Trypsin Kinetic energy Bovine Pancreatic Trypsin Inhibitor Enzyme Reaction rate constant chemistry medicine biology.protein Basic Pancreatic Trypsin Inhibitor medicine.drug
Zdroj:	Bayer-Symposium ISBN: 9783642879685
Popis:	Recently Luthy et al [1] investigated the mechanism of the interaction between soybean trypsin inhibitor (STI)1 and trypsin by kinetic methods. These authors found that only at very low reactant concentration the reaction is second order with rate constants k on and k off. Significant deviation at higher total enzyme and inhibitor concentrations lead to the postulation of a more complex mechanism with an intermediate complex L which is in fast pre-equilibrium with enzyme E and inhibitor I
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::8457881d0bed07a7593f0d124fe246e3 https://doi.org/10.1007/978-3-642-87966-1_46 Zobrazit plný text záznamu