The use of auramine 0 to study ligand binding and subunit cooperativity of lactate dehydrogenase-Reference-Cited by-同舟云学术

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The use of auramine 0 to study ligand binding and subunit cooperativity of lactate dehydrogenase

Published:1984-09 Issue:2 Volume:789 Page:216-223
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Ivanov M.V.,Kube D.,Nagradova N.K.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference31 articles.

1. The effect of oligomeric environment on the kinetics of lactate dehydrogenase subunits

2. Characterization of a fluorescent complex between auramine O and horse liver alcohol dehydrogenase

3. Relation of the auramine O binding site to the active site of horse liver alcohol dehydrogenase

Cited by 4 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. A Protein Biosensor for Lactate;Analytical Biochemistry;2000-07

2. Protein-ligand interactions. 6 nicotinic acetylcholine receptor agonist activity of isoquinoline alkaloids;Bioorganic & Medicinal Chemistry Letters;1996-12

3. Interaction between D-glyceraldehyde-3-phosphate dehydrogenase and 3-phosphoglycerate kinase labeled by fluorescein-5′-isothiocyanate: Evidence that the dye participates in the interaction;Biochemical and Biophysical Research Communications;1989-05

4. High resolution of human lactate dehydrogenase: New multiple forms and potential tumor markers;Electrophoresis;1988

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