Influence Of Monovalent Ions Research Articles

50 Years since Kaufman and Phillips’ Groundbreaking Trilogy Elucidating Ion and Water Homeostasis in Ixodid Ticks

The enormous volume of blood ingested by hard ticks during their long attachment period is without a doubt the hallmark of their biology. Maintaining a homeostatic balance between ion and water intake and loss during their feeding is critical to preventing osmotic stress and death. Exactly 50 years ago, Kaufman and Phillips published a series of three consecutive papers on "Ion and water balance in the ixodid tick Dermacentor andersoni", Journal of Experimental Biology (1973): I. Routes of ion and water excretion, 58: 523-36; II. Mechanism and control of salivary secretion 58: 537-547; and III. Influence of monovalent ions and osmotic pressure on salivary secretion 58: 549-564. This classic series significantly expanded our knowledge of the unique regulatory processes governing ion and water balance in fed ixodid ticks, highlighting its uniqueness among the blood-feeding arthropods. Their pioneer work had an enormous impact on understanding the vital role of salivary glands in these actions, and ultimately provided a consequential stepping stone for a new era of hard tick salivary gland physiological research.

Influence of monovalent ions on density fluctuations in hydrothermal aqueous solutions by small angle X-ray scattering

Synchrotron small angle X-ray scattering measurements on water and alkaline bromine aqueous solutions (XBr, with X = Li, Rb, or Cs) were carried out from ambient to supercritical conditions. The temperature was increased from 300 to 750 K along several isobars between 24 and 35 MPa. The correlation length and the structure factor were extracted from the data following the Ornstein-Zernike formalism. We obtained experimental evidence of the shift of the critical point and isochore and their dependence on the ions concentration (0.33 mol/kg and 1.0 mol/kg). We also observed that the size of the density fluctuations and the structure factor increase with the presence of the ions and that this effect is positively correlated with the atomic number of the cation. These behaviors were compared with ZnBr(2) and NaCl systems from the literature.

Influence of monovalent ions on the activity of the (Ca 2+ + Mg 2+)-ATPase and Ca 2+-transport of human red blood cells

In reconstituted human red blood cells a difference was found in (Ca 2+ + Mg 2+)-ATPase activity and in Ca 2+ efflux at 37°C, depending on the side of the membrane at which the monovalent cations K + and Na + were placed. Under the conditions used, (Ca 2+ + Mg 2+)-ATPase activity and Ca 2+ efflux was highest when K + ( 35 ± 0.5 mM (± S.E.) , mean of four experiments) was at the inside and Na + (130 mM) at the outside of the ghost membrane.

Glutamyl transfer ribonucleic acid synthetase of Escherichia coli. Study of the interactions with its substrates

The binding of the various substrates to Escherichia coli glutamyl-tRNA synthetase has been investigated by using as experimental approaches the binding study under equilibrium conditions and the substrate-induced protection of the enzyme against its thermal inactivation. The results show that ATP and tRNAGlu bind to the free enzyme, whereas glutamate binds only to an enzyme form to which glutamate-accepting tRNAGlu is associated. By use of modified E. coli tRNAsGlu and heterologous tRNAsGlu, a correlation could be established between the ability of tRNAGlu to be aminoacylated by glutamyl-tRNA synthetase and its abilities to promote the [32P]PPi-ATP isotope exchange and the binding of glutamate to the synthetase. These results give a possible explanation for the inability of blutamyl-tRNA synthetase to catalyze the isotope exchange in the absence of amino acid accepting tRNAGlu and for the failure to detect an enzyme-adenylate complex for this synthetase by using the usual approaches. One binding site was detected for each substrate. The specificity of the interaction of the various substrates has been further investigated. Concerning ATP, inhibition studies of the aminoacylation reaction by various analogues showed the existence of a synergistic effect between the adenine and the ribose residues for the interaction of adenosine. The primary recognition of ATP involves the N-1 and the 6-amino group of adenine as well as the 2'-OH group of ribose. This first interaction is then strengthened by the phosphate groups- Inhibition studies by various analogues of glutamate showed a strong decrease in the affinity of this substrate for the synthetase after substitution of the alpha- or gamma-carboxyl groups. The enzyme exhibits a marked tendency to complex tRNAs of other specificities even in the presence of tRNAGlu. MgCl2 and spermidine favor the specific interactions. The influence of monovalent ions and of pH on the interaction between glutamyl-tRNA synthetase and tRNAGlu is similar to those reported for other synthetases not requiring their cognate tRNA to bind the amino acid. Finally, contrary to that reported for other monomeric synthetases, no dimerization of glutamyl-tRNA synthetase occurs during the catalytic process.