Continuous fluorimetric assay of 5′-nucleotidase with formycin 5′-phosphate as substrate, and its application to properties of substrates and inhibitors
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference28 articles.
1. Preparation and Properties of 5'-Nucleotidase from Smooth Muscle of Small Intestine
2. Sensitive Fluorimetric Assay for Adenosine Deaminase with Formycin as Substrate; and Substrate and Inhibitor Properties of some Pyrazolopyrimidine and Related Analogues
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1. Identification of guanine, guanosine, and inosine for α-amylase inhibitors in the extracts of the earthworm Eisenia fetida and characterization of their inhibitory activities against porcine pancreatic α-amylase;Enzyme and Microbial Technology;2020-12
2. 1,N6-ethenoadenine and other Fluorescent Nucleobase Analogs as Substrates for Purine-Nucleoside Phosphorylases: Spectroscopic and Kinetic Studies;Current Pharmaceutical Design;2018-02-16
3. Identification of the tautomeric form of formycin A in its complex with Escherichia coli purine nucleoside phosphorylase based on the effect of enzyme–ligand binding on fluorescence and phosphorescence;European Biophysics Journal;2003-12-04
4. Emission Spectroscopy of Complex Formation between Escherichia coli Purine Nucleoside Phosphorylase (PNP) and Identified Tautomeric Species of Formycin Inhibitors Resolves Ambiguities Found in Crystallographic Studies;Fluorescence Spectroscopy, Imaging and Probes;2002
5. Formycin A and its N-methyl analogues, specific inhibitors of E. coli purine nucleoside phosphorylase (PNP): induced tautomeric shifts on binding to enzyme, and enzyme→ligand fluorescence resonance energy transfer;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;2000-01
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