Adjustment of K' for the creatine kinase, adenylate kinase and ATP hydrolysis equilibria to varying temperature and ionic strength.

1996 ◽  
Vol 199 (2) ◽  
pp. 509-512 ◽  
Author(s):  
W E Teague ◽  
E M Golding ◽  
G P Dobson
Keyword(s):  
Creatine Kinase ◽  
Ionic Strength ◽  
Adenylate Kinase ◽  
Atp Hydrolysis ◽  
Equilibrium Constants ◽  
Experimental Conditions ◽  
Physiological Conditions ◽  
Free Energy Of Formation ◽  
Apparent Equilibrium ◽  
Energy Of Formation

Comparative physiologists and biochemists working with tissues at varying temperatures and ionic strength are required to adjust apparent equilibrium constants (K') of biochemical reactions to the experimental conditions prior to calculating cytosolic bioenergetic parameters (transformed Gibbs free energy of formation, DeltafG' ATP; cytosolic phosphorylation ratio, [ATP]/[ADP][Pi]; [phosphocreatine]: [orthophosphate] ratio [PCr]/[Pi]) and kinetic parameters (free [ADP], [Pi] and [AMP]). The present study shows how to adjust both K' and the equilibrium constants of reference reactions (Kref) of creatine kinase (ATP: creatine N-phosphotransferase; EC 2.7.3.2), adenylate kinase (ATP:AMP phosphotransferase; EC 2.7.4.3) and adenosinetriphosphatase (ATP phosphohydrolase; EC 3.6.1.3) to temperature and ionic strength. This information, together with our previous study showing how to adjust equilibria to varying pH and pMg, is vital for the quantification of organ and tissue bioenergetics of ectotherms and endotherms under physiological conditions.

scholarly journals Adjustment of K' to varying pH and pMg for the creatine kinase, adenylate kinase and ATP hydrolysis equilibria permitting quantitative bioenergetic assessment.

1995 ◽  
Vol 198 (8) ◽  
pp. 1775-1782 ◽  
Author(s):  
E M Golding ◽  
W E Teague ◽  
G P Dobson
Keyword(s):  
Creatine Kinase ◽  
Gibbs Energy ◽  
Adenylate Kinase ◽  
Atp Hydrolysis ◽  
Equilibrium Constants ◽  
Binding Constants ◽  
Acid Dissociation ◽  
Free Magnesium ◽  
Apparent Equilibrium ◽  
Energy Of Formation

Physiologists and biochemists frequently ignore the importance of adjusting equilibrium constants to the ionic conditions of the cell prior to calculating a number of bioenergetic and kinetic parameters. The present study examines the effect of pH and free magnesium levels (free [Mg2+]) on the apparent equilibrium constants (K') of creatine kinase (ATP: creatine N-phosphotransferase; EC 2.7.3.2), adenylate kinase (ATP:AMP phosphotransferase; EC 2.7.4.3) and adenosinetriphosphatase (ATP phosphohydrolase; EC 3.6.1.3) reactions. We show how K' can be calculated using the equilibrium constant of a specified chemical reaction (Kref) and the appropriate acid-dissociation and Mg(2+)-binding constants at an ionic strength (I) of 0.25 mol l-1 and 38 degrees C. Substituting the experimentally determined intracellular pH and free [Mg2+] into the equation containing a known Kref and two variables, pH and free [Mg2+], enables K' to be calculated at the experimental ionic conditions. Knowledge of K' permits calculation of cytosolic phosphorylation ratio ([ATP]/[ADP][Pi]), cytosolic free [ADP], free [AMP], standard transformed Gibbs energy of formation (delta fG' degrees ATP) and the transformed Gibbs energy of the system (delta fG' ATP) for the biological system. Such information is vital for the quantification of organ and tissue bioenergetics under physiological and pathophysiological conditions.

Tautomeric equilibria and pKa values for 'sulfurous acid' in aqueous solution: a thermodynamic analysis

1979 ◽  
Vol 57 (4) ◽  
pp. 454-457 ◽  
Author(s):  
J. Peter Guthrie
Keyword(s):  
Aqueous Solution ◽  
Free Energy ◽  
Aqueous Solutions ◽  
Equilibrium Constants ◽  
Acid Solutions ◽  
Sulfurous Acid ◽  
Free Energy Of Formation ◽  
Dilute Aqueous Solutions ◽  
Sulfite Ion ◽  
Energy Of Formation

The free energy of formation of dimethyl sulfite in aqueous solution can be calculated as −91.45 ± 0.79 kcal/mol; this calculation required measurement of the solubility of dimethyl sulfite. From this value and the pKa of SO(OH)2, using previously reported methods, the free energy of formation of SO(OH)2 can be calculated to be −129.26 ± 0.89 kcal/mol. Comparison of this value with the value obtained from the free energy of formation of 'sulfurous acid' solutions, calculated from the free energy of formation of sulfite ion and the apparent pKa, values, permits evaluation of the free energy of covalent hydration of SO2 as 1.6 + 1.0 kcal/mol, in agreement with earlier qualitative spectroscopic observations. From the apparent pKa and the anticipated pKa values for the tautomers (SO(OH)2, pK1 = 2.3; HSO2(OH), pK1 = −2.6) it is possible to calculate the free energy change for tautomerization of SO(OH)2 to H—SO2(OH) as +4.5 ± 1.2 kcal/mol. All equilibrium constants required for Scheme 1, describing the species present in dilute aqueous solutions of SO2, have been calculated. In agreement with previous Raman studies the major tautomer of 'bisulfite ion' is calculated to be H—SO3−.

The Solubility of Metallic Selenium under Anoxic Conditions

2000 ◽  
Vol 663 ◽  
Author(s):  
Yoshihisa Iida ◽  
Tetsuji Yamaguchi ◽  
Shinichi Nakayama ◽  
Tomoko Nakajima ◽  
Yoshiaki Sakamoto
Keyword(s):  
Free Energy ◽  
Solid Phase ◽  
Equilibrium Constants ◽  
Absorption Spectrometry ◽  
X Ray Diffraction ◽  
Molar Free Energy ◽  
Anoxic Conditions ◽  
X Ray ◽  
Free Energy Of Formation ◽  
Energy Of Formation

ABSTRACTThe solubility of metallic selenium was measured in a mixture of 0.1M-NaCl and 0.05M-N2H4under anoxic conditions (O2 < 1 ppm) by both oversaturation and undersaturation methods. Equilibrium was attained in 40 days. The aqueous selenium species identified were HSe at pH between 5 and 8, and Se42at pH between 10 and 13, by UV-Vis absorption spectrometry. The solid phase was identified as Se (cr) by X-ray diffraction. The equilibrium constants ofSe(cr) + H+ + 2e- = HSe- logK0 = -6.5±0.5 and4Se(cr) + 2e- = Se42- logK0 = -16.8±0.5were determined. The standard molar free energy of formation of HSe- and Se42-was determined to be (37.1±2.9) and (95.9±2.9) kJ/mol, respectively.

Phosphocreatine represents a thermodynamic and functional improvement over other muscle phosphagens

1989 ◽  
Vol 143 (1) ◽  
pp. 177-194 ◽  
Author(s):  
W. R. Ellington
Keyword(s):  
31P Nmr ◽  
Creatine Phosphokinase ◽  
Equilibrium Constants ◽  
Functional Improvement ◽  
Intracellular Acidosis ◽  
K Value ◽  
Physiological Conditions ◽  
Vertebrate Muscle ◽  
Nmr Methods ◽  
Apparent Equilibrium

In vertebrate tissues, the only phosphagen is phosphocreatine (PC), and the corresponding phosphotransferase is creatine phosphokinase (CPK). Among invertebrates, a variety of phosphotransferase reactions are found in addition to CPK, including arginine phosphokinase (APK), glycocyamine phosphokinase (GPK), taurocyamine phosphokinase (TPK) and lombricine phosphokinase (LPK). Although there is some uncertainty about the exact value, the apparent equilibrium constant for the CPK reaction (K′cpk = [creatine][ATP]/[PC][ADP]), under physiological conditions similar to those of vertebrate muscle, ranges from 100 to 160. The corresponding K′ value for the APK reaction is somewhat controversial, and K′ values for the GPK. TPK and LPK reactions are not known. In this study, conventional and 31P-NMR methods were used to evaluate the equilibrium constants for the APK, GPK, TPK and LPK reactions relative to that of CPK. The corresponding K′ values for the APK, GPK, TPK and LPK reactions, expressed as a percentage of K′cpk, are 13, 29, 29 and 32%, respectively. The exclusively invertebrate phosphagens exist as a cohort of thermodynamically more stable compounds. Thus, PC constitutes a thermodynamic (and functional) improvement, in that the CPK reaction is able to buffer ATP at much higher ATP/ADP ratios than are other phosphagens. However, possession of a phosphagen system with a lower K′ value may be advantageous under certain specific physiological conditions such as intracellular acidosis.

Equilibrium in the formation of barium carbonate from barium sulphate

1976 ◽  
Vol 54 (24) ◽  
pp. 3872-3875
Author(s):  
Harry Horlings ◽  
Donald S. Scott ◽  
John R. Wynnyckyj
Keyword(s):  
Free Energy ◽  
Barium Carbonate ◽  
Equilibrium Constants ◽  
Barium Sulphate ◽  
Heat Of Reaction ◽  
Temperature Range ◽  
Free Energy Of Formation ◽  
Energy Of Formation

Heat of reaction and free energy of formation at 25 °C were determined from experimental equilibrium yields for the reaction[Formula: see text]in an aqueous solution.The values are 5045 and 1927 cal/mol respectively. Equilibrium constants for the reaction were determined over a temperature range from 20 to 193 °C.

Interaction of Plasminogen Activators and Plasminogen with Heparin: Effect of Ionic Strength

1993 ◽  
Vol 70 (05) ◽  
pp. 867-872 ◽  
Author(s):  
Dingeman C Rijken ◽  
Gerard A W de Munk ◽  
Annie F H Jie
Keyword(s):  
Molecular Weight ◽  
Ionic Strength ◽  
Plasminogen Activator ◽  
Plasminogen Activators ◽  
Fibrinolytic System ◽  
Tissue Type ◽  
Single Chain ◽  
Physiological Conditions ◽  
Amino Terminal ◽  
Type Plasminogen Activator

SummaryIn order to define the possible effects of heparin on the fibrinolytic system under physiological conditions, we studied the interactions of this drug with plasminogen and its activators at various ionic strengths. As reported in recent literature, heparin stimulated the activation of Lys-plasminogen by high molecular weight (HMW) and low molecular weight (LMW) two-chain urokinase-type plasminogen activator (u-PA) and two-chain tissue-type plasminogen activator (t-PA) 10- to 17-fold. Our results showed, however, that this stimulation only occurred at low ionic strength and was negligible at a physiological salt concentration. Direct binding studies were performed using heparin-agarose column chromatography. The interaction between heparin and Lys-plasminogen appeared to be salt sensitive, which explains at least in part why heparin did not stimulate plasminogen activation at 0.15 M NaCl. The binding of u-PA and t-PA to heparinagarose was less salt sensitive. Results were consistent with heparin binding sites on both LMW u-PA and the amino-terminal part of HMW u-PA. Single-chain t-PA bound more avidly than two-chain t-PA. The interactions between heparin and plasminogen activators can occur under physiological conditions and may modulate the fibrinolytic system.

scholarly journals The Effect of pH, Ionic Strength and the Presence of PbII on the Formation of Calcium Carbonate from Homogenous Alkaline Solutions at Room Temperature

Minerals ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 783
Author(s):  
Fulvio Di Lorenzo ◽  
Kay Steiner ◽  
Sergey V. Churakov
Keyword(s):  
Ionic Strength ◽  
Deep Understanding ◽  
Inhibitory Effect ◽  
Alkaline Solutions ◽  
Nucleation Kinetics ◽  
Experimental Conditions ◽  
Calcium Carbonates ◽  
Natural Systems ◽  
Geological Processes ◽  
System Variables

Precipitation of calcium carbonates in aqueous systems is an important factor controlling various industrial, biological, and geological processes. In the first part of this study, the well-known titration approach introduced by Gebauer and coworkers in 2008 s used to obtain reliable experimental dataset for the deep understanding of CaCO3 nucleation kinetics in supersaturated solutions over a broad range of pH and ionic strength conditions. In the second part, the effect of impurities, i.e., 1 mol% of Pb2+, was assessed in the same range of experimental conditions. Divalent lead has been shown to have an inhibitory effect in all ranges of the conditions tested except for pH 8 and low ionic strength (≤0.15 mol/L). Future investigations might take advantage of the methodology and the data provided in this work to investigate the effect of other system variables. The investigation of all the major variables and the assessment of eventual synergic effects could improve our ability to predict the formation of CaCO3 in complex natural systems.

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