Boric Acid Inhibits Adenosine Diphosphate-Ribosyl Cyclase Non-Competitively
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2006/05/19
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Description:Adenosine diphosphate-ribosyl cyclase (ADP-ribosyl cyclase) is a ubiquitous enzyme in eukaryotes that converts NAD+ to cyclic-ADP-ribose (cADPR) and nicotinamide. A quantitative assay for cADPR was developed using capillary electrophoresis to separate NAD+, cADPR, ADP-ribose, and ADP with UV detection (254 nm). Using this assay, the apparent Km and Vmax for Aplysia ADP-ribosyl cyclase were determined to be 1.24 +/- 0.05 mM and 131.8 +/- 2.0 uM/min, respectively. Boric acid inhibited ADP-ribosyl cyclase non-competitively with a Ki of 40.5 +/- 0.5 mM. Boric acid binding to cADPR, determined by electrospray ionization mass spectrometry, was characterized by an apparent binding constant, KA, of 655 +/- 99 L/mol at pH 10.3. [Description provided by NIOSH]
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ISSN:0021-9673
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Pages in Document:246-252
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Volume:1115
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Issue:1
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NIOSHTIC Number:nn:20058366
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Citation:J Chromatogr A 2006 May; 1115(1-2):246-252
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Contact Point Address:Curtis D. Eckhert, Department of Environmental Health Sciences, Box 951772, University of California, 650 Charles E Young Dr South, Los Angeles, CA 90095-1772, USA
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Email:ceckhert@ucla.edu
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Federal Fiscal Year:2006
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Performing Organization:University of California Los Angeles
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Peer Reviewed:True
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Start Date:20050701
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Source Full Name:Journal of Chromatography A
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End Date:20270630
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Main Document Checksum:urn:sha-512:5cdc2a22899ee79f16be5dea46d5d5af9a45bea8d68cb33e366a0344ff2e386a0bab6356c3075d01e4bc173abd1d00ac49c9b88329b63f5bbf9961913354236d
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