Divalent cations, such as calcium and magnesium, are constantly present in extracellular compartment of most organisms. Modification of extracellular concentrations of divalent ions causes changes in physiologic functions, such as excitability and conduction of the nerves. The present study was designed to investigate and compare the effects of calcium and magnesium on nerve conduction and lido...

The subcellular distribution of neutral sphingomyelinase activity has been determined in rat liver. Neutral sphingomyelinase is present in the plasma membrane. This enzyme requires either Mg2+ or Mn2+ for full activity; these cations cannot be replaced by Co2+ or Ca2+. The plasma membrane sphingomyelinase is strongly inhibited by Hg2+. A small amount of neutral spingomyelinase activity appears ...

We have begun to identify and characterize genes that are differentially expressed with low magnesium. One of these sequences conformed to the solute carrier SLC41A1. Real-time RT-PCR of RNA isolated from renal distal tubule epithelial [mouse distal convoluted tubule (MDCT)] cells cultured in low-magnesium media relative to normal media and in the kidney cortex of mice maintained on low-magnesi...

Millimolar concentrations of monovalent cations enhance and divalent cations impede the redistribution (spill-over) of electronic excitation energy from Photosystem (PS) II to PS I in cation-depleted (sucrose-washed) thylakoids; this concept is based on chlorophyll a fluorescence and electron transport measurements over a narrow pH range around 7. We have tested the above concept in pea thylako...

Fructose-1,6-bisphosphatase requires divalent cations (Mg2+, Mn2+, or Zn2+) for catalysis, but a diverse set of monovalent cations (K+, Tl+, Rb+, or NH(4)(+)) will further enhance enzyme activity. Here, the interaction of Tl+ with fructose-1,6-bisphosphatase is explored under conditions that support catalysis. On the basis of initial velocity kinetics, Tl+ enhances catalysis by 20% with a K(a) ...

At neutral pH, Zn2+ is a potent and specific inhibitor of rat liver fructose 1,6-bisphosphatase (EC 3.1.3.11; D-fructose-1,6-bisphosphate 1-phosphohydrolase). Inhibition by Zn2+ is uncompetitive with respect to the activating cations Mg2+ and Mn2+, and the kinetic data suggest that the enzyme possesses a distinct high-affinity binding site for Zn2+, with Ki of approximately 0.3 muM. At higher c...

The enzymatic activity of citrate synthase from pig heart can be inhibited by various ions. The order of inhibitory effect of monovalent cations is Li+ > K+ > Na+ > Cs+ and that of anions is SCN> Cl> tartrate. Divalent cations such as Ca2+ and Mg2+ are much more effective than monovalent cations, but thiocyanate is as effective as divalent cations. ATP is also a potent inhibitor, but dATP has n...

Effects of monovalent cations on the neutral rabbit liver fructose-1,6-bisphosphatase are multifunctional and dependent on their nonhydrated ionic size. (a) The maximal velocity is increased by addition of monovalent cations with the optimum stimulation occurring with a nonhydrated ionic radius of 1.2 A in the presence of a chelating agent such as EDTA. (B) Activation curves are sigmoidal with ...

Extracellular magnesium ions [Mg2+]o are known to regulate functions of endothelial cells, but whether [Mg2+]o can alter intracellular free ionized magnesium [Mg2+]i in these cells remains unknown. The present studies, using digital imaging microscopy and the Mg2+ fluorescent probe, mag-fura-2, determined effects of elevation of [Mg2+]o on [Mg2+]i in cultured human aortic endothelial cells. Wit...