Influence of substrate and effectors on the binding of 1-anilino-8-naphthalenesulfonate by glycogen phosphorylase
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00755a006
Reference38 articles.
1. Substrate-induced Conformational Changes of Liver Fructose 1,6-Diphosphatase Studied with the Hydrophobic Probe, 1-Anilinonaphthalene-8-sulfonate
2. Comparative Studies on Glycogen Phosphorylase
3. Structural and Catalytic Properties of Lobster Muscle Glycogen Phosphorylase
4. Probes for the Conformational Transitions of Phosphorylase b. Effect of Ligands Studied by Proton Relaxation Enhancement, Fluorescence and Chemical Reactivities
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1. Binding of 9-Anthroylcholine Monitors the Interactions of Adenosine Cyclic 3′,5′-Phosphate-dependent Protein Kinase with MgATP, Substrates, and Regulatory Subunits;Journal of Biological Chemistry;1998-12
2. Continuous Enzymatic Assay for Phosphorylase Kinase in a Monocascade Enzyme System;Analytical Biochemistry;1997-01
3. Preparation and functional characterization of a catalytically active fragment of phosphorylase kinase;Molecular and Cellular Biochemistry;1993-11
4. Preparation and functional characterization of a catalytically active fragment of phosphorylase kinase;Reversible Protein Phosphorylation in Cell Regulation;1993
5. Phosphorylase kinase: Development of a continuous fluorometric assay for the determination of catalytic activity;Biochemical and Biophysical Research Communications;1991-01
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