INTERACTION IN SALT VAPORS AND ACTIVITY COEFFICIENTS IN THE POTASSIUM CHLORIDE—MAGNESIUM CHLORIDE SYSTEM1,2

1963 ◽  
Vol 67 (6) ◽  
pp. 1259-1263 ◽  
Author(s):  
Eugene E. Schrier ◽  
Herbert M. Clark

1993 ◽  
Vol 14 (2) ◽  
pp. 172-178 ◽  
Author(s):  
G. S. Perry ◽  
H. Fletcher


1970 ◽  
Vol 120 (1) ◽  
pp. 15-24 ◽  
Author(s):  
P. S. G. Goldfarb ◽  
R. Rodnight

1. The intrinsic Na+, K+, Mg2+ and Ca2+ contents of a preparation of membrane fragments from ox brain were determined by emission flame photometry. 2. Centrifugal washing of the preparation with imidazole-buffered EDTA solutions decreased the bound Na+ from 90±20 to 24±12, the bound K+ from 27±3 to 7±2, the bound Mg2+ from 20±2 to 3±1 and the bound calcium from 8±1 to <1nmol/mg of protein. 3. The activities of the Na++K++Mg2+-stimulated adenosine triphosphatase and the Na+-dependent reaction forming bound phosphate were compared in the unwashed and washed preparations at an ATP concentration of 2.5μm (ATP/protein ratio 12.5pmol/μg). 4. The Na+-dependent hydrolysis of ATP as well as the plateau concentration of bound phosphate and the rate of dephosphorylation were decreased in the washed preparation. The time-course of formation and decline of bound phosphate was fully restored by the addition of 2.5μm-magnesium chloride and 2μm-potassium chloride. Addition of 2.5μm-magnesium chloride alone fully restored the plateau concentration of bound phosphate, but the rate of dephosphorylation was only slightly increased. Na+-dependent ATP hydrolysis was partly restored with 2.5μm-magnesium chloride; addition of K+ in the range 2–10μm-potassium chloride then further restored hydrolysis but not to the control rate. 5. Pretreatment of the washed preparation at 0°C with 0.5nmol of K+/mg of protein so that the final added K+ in the reaction mixture was 0.1μm restored the Na+-dependent hydrolysis of ATP and the time-course of the reaction forming bound phosphate. 6. The binding of [42K]potassium chloride by the washed membrane preparation was examined. Binding in a solution containing 10nmol of K+/mg of protein was linear over a period of 20min and was inhibited by Na+. Half-maximal inhibition of 42K+-binding required a 100-fold excess of sodium chloride. 7. It was concluded (a) that a significant fraction of the apparent Na+-dependent hydrolysis of ATP observed in the unwashed preparation is due to activation by bound K+ and Mg2+ of the Na++K++Mg2+-stimulated adenosine triphosphatase system and (b) that the enzyme system is able to bind K+ from a solution of 0.5μm-potassium chloride.







2020 ◽  
Vol 80 (2) ◽  
pp. 285-289
Author(s):  
R. Stefanello ◽  
B. B. Viana ◽  
P. C. H. Goergen ◽  
L. A. S. Neves ◽  
U. R. Nunes

Abstract Salinity, of both soil and water, is one of the main causes of crop yield decline. Within this context, the objective of this study was to evaluate the influence of different salts on the germination of chia seeds. The experiment was conducted in a BOD chamber at a constant temperature of 20 °C and in the presence of light. The seeds were placed on paper soaked with aqueous solutions of calcium chloride (CaCl2), sodium chloride (NaCl), potassium chloride (KCl), and magnesium chloride (MgCl2), at the osmotic potentials zero, -0.10, -0.20, -0.30, and -0.40 MPa. The effect of the salinity was evaluated using a germination test, with counts on days 7 and 14 after sowing. Based on the results, chia seeds tolerate concentrations of NaCl to -0.4 MPa and KCl to -0.20 MPa. The salts CaCl2 and MgCl2 had a negative effect on the germination and vigor of the chia seeds for the osmotic potentials -0.30 MPa and -0.20 MPa, respectively.



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