| Literature DB >> 16545389 |
Danny H Kim1, Shane Que Hee, Andrew J Norris, Kym F Faull, Curtis D Eckhert.
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.Entities:
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Year: 2006 PMID： 16545389 DOI： 10.1016/j.chroma.2006.02.066
Source DB: PubMed Journal: J Chromatogr A ISSN： 0021-9673 Impact factor: 4.759