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J Chromatogr A. 2006 May 19;1115(1-2):246-52. Epub 2006 Mar 20.

Boric acid inhibits adenosine diphosphate-ribosyl cyclase non-competitively.

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1
Department of Environmental Health Sciences, Box 951772, University of California, 650 Charles E Young Dr South, Los Angeles, CA 90095-1772, USA.

Abstract

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 microM/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.

PMID:
16545389
DOI:
10.1016/j.chroma.2006.02.066
[Indexed for MEDLINE]
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