A pH-induced change in state around active-site tryptophan residues of Rhizopus niveus glucoamylase, detected by stopped-flow studies of chemical modification with N-bromosuccinimide-Reference-Cited by-同舟云学术

A pH-induced change in state around active-site tryptophan residues of Rhizopus niveus glucoamylase, detected by stopped-flow studies of chemical modification with N-bromosuccinimide

Published:1990-03 Issue: Volume:197 Page:237-244
ISSN:0008-6215
Container-title:Carbohydrate Research
language:en
Short-container-title:Carbohydrate Research

Author:

Ohnishi Masatake,Nakamura Yuki,Murata-Nakai Masako,Hiromi Keitaro

Publisher

Elsevier BV

Subject

Organic Chemistry,Biochemistry,General Medicine,Analytical Chemistry

Reference15 articles.

1. Kinetic Studies on the Chemical Modification of Lysozyme by N-Bromosuccinimide and Its Protection by Substrates and Analogs1

2. Stopped-flow chemical modification with N-bromosuccinimide: A good probe for changes in the microenvironment of the Trp 62 residue of chicken egg white lysozyme

3. Kinetic discrimination of tryptophan residues of glucoamylase from Rhizopus niveus by fast chemical modification with N-bromosuccinimide

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1. Amylolytic Enzymes;Food Enzymes;1995

2. Cycloamylose Glucanotransferase-catalyzed Cyclisation for a Substrate Maltose. Modification with N-Bromosuccimide on the Tryptophan Residues;Starch - Stärke;1994

3. Effect of modification of the tryptophan residues of cyclodextrin glucanotransferase with N-bromosuccinimide on the enzyme-catalysed hydrolysis (cleavage) of soluble starch and cyclomaltohexaose;Carbohydrate Research;1992-04

4. Roles of the aromatic side chains in the binding of substrates, inhibitors, and cyclomalto-oligosaccharides to the glucoamylase from Aspergillus niger probed by perturbation difference spectroscopy, chemical modification, and mutagenesis;Carbohydrate Research;1992-04