Abstract
The Hsp90 molecular chaperone is responsible for the conformational maturation of nascent polypeptides and the rematuration of denatured proteins. Inhibition of Hsp90 represents a promising approach towards the treatment of cancer because numerous signaling cascades can be simultaneously targeted by disruption of the Hsp90-mediated process. Hsp90's ATPase activity is essential to the Hsp90-mediated protein folding process, consequently, a coupled assay was developed and optimized for determination of Hsp90's inherent ATPase activity. Using maltose phosphorylase, glucose oxidase, and horseradish peroxidase as components of this assay, a highly reproducible assay with a Z-factor of 0.87 has been produced.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases / analysis
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Adenosine Triphosphatases / antagonists & inhibitors
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Adenosine Triphosphatases / isolation & purification
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Adenosine Triphosphatases / metabolism*
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Adenosine Triphosphate / metabolism*
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Adenosine Triphosphate / pharmacology
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Catalysis
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Glucose Oxidase / metabolism
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Glucosyltransferases / metabolism
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HSP90 Heat-Shock Proteins / analysis
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HSP90 Heat-Shock Proteins / antagonists & inhibitors
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HSP90 Heat-Shock Proteins / isolation & purification
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HSP90 Heat-Shock Proteins / metabolism*
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Horseradish Peroxidase / metabolism
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Hydrogen Peroxide / pharmacology
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Molecular Structure
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Reproducibility of Results
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Temperature
Substances
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HSP90 Heat-Shock Proteins
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Adenosine Triphosphate
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Hydrogen Peroxide
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Glucose Oxidase
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Horseradish Peroxidase
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Glucosyltransferases
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maltose phosphorylase
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Adenosine Triphosphatases