Transducin-activated cGMP-specific phosphodiesterase of external segments of bovine retinal rods: The influence of magnesium ions

The kinetic behavior of phosphodiesterase activated by transducin in a complex with a non-hydrolyzable GTP analogue (guanosine-5′-O-thiotriphosphate) was studied by the pH-metric method in preparations of light-adapted external segments of bovine retinal rods in a range of magnesium ion concentratio...

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Published inBiophysics (Oxford) Vol. 61; no. 6; pp. 877 - 879
Main Authors Petrukhin, O. V., Orlova, T. G., Nezvetsky, A. R., Orlov, N. Ya
Format Journal Article
LanguageEnglish
Published Moscow Pleiades Publishing 01.11.2016
Springer Nature B.V
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Summary:The kinetic behavior of phosphodiesterase activated by transducin in a complex with a non-hydrolyzable GTP analogue (guanosine-5′-O-thiotriphosphate) was studied by the pH-metric method in preparations of light-adapted external segments of bovine retinal rods in a range of magnesium ion concentrations from 0.4 to 20 mM. These results indicate that when using the reaction media containing 10–15 mM Mg 2+ ions, introduction of 2–4 mM ethylene glycol tetraacetic acid (a chelator of calcium ions) in the reaction medium induces only relatively small changes in the concentration of free magnesium ions that are not able to significantly influence the phosphodiesterase activity.
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ISSN:0006-3509
1555-6654
DOI:10.1134/S0006350916050237