PubMed · 5826355
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A K Basu, S Gupta, A Haq, N Islam, C Banerjee. 1965-08-01. Extracorporeal circulation.. https://pubmed.ncbi.nlm.nih.gov/5826355/
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The binding of hydrogen ions and magnesium ions by a biochemical reactant, like ATP, can be calculated by writing the binding polynomial (partition function) Q and taking the partial derivatives of log Q with respect to pH and pMg by use of a mathematical program in a personal computer. The change in binding of hydrogen ions and magnesium ions in a biochemical reaction, like the hydrolysis of ATP, can be calculated by taking the partial derivatives of log (K'/K), where K' is the apparent equilibrium constant and K is the equilibrium constant for a reference chemical reaction. These calculations can be checked by using the computer to calculate the mixed partial derivatives, which must be equal. The effects of pH, pMg, and ionic strength on the changes in binding in the hydrolysis of ATP are calculated. At 298.15 K, pH7, pMg 3, and 0.25 M ionic strength, the hydrolysis of ATP to ADP and inorganic phosphate liberates 0.62 mol of hydrogen ions and 0.45 mol of magnesium ions into the medium.
Interaction of H(+)-ions with alpha-crystallin from goat lens has been studied at three different ionic strengths using the potentiometric titration method. Titrations have also been carried out in the presence of 1.5 M and 6 M GuHCl (guanidine hydrochloride). The isoionic pH of the protein in water and the effect of KCl on it have been determined. Titration curves have been found to be reversible between pH 3 to 9.25 at all ionic strengths. To aid in the data analyses, the reactivities of alpha-crystallin lysine residues to trinitrobenzenesulfonic acid have been determined in this work. For alpha-crystallin aggregate, 130 +/- 2 histidine side chains out of a total of 300 and about 134 +/- 4 lysine side chains out of 310 have been found to be inaccessible to the solvent in the native condition. The remaining titratable side chains determine the surface charge of the native protein. In 1.5 M GuHC1, however, the nontitratable histidine side chains are found to be available for titration as are the nontitratable lysine and tyrosine side chains in 6M GuHC1. The theoretical titration curve computed on the basis of Linderstrøm-Lang model is found to fit quite comfortably with the experimental one between pH 4.6 and 9.25. The pKint value for beta gamma-carboxyl side chains has been found to be 5.18 which is somewhat higher than usual indicating that the carboxyl groups in the protein are probably in some constrained condition which is released in the presence of a denaturant. Below pH 4.6, there begins a conformational change in the alpha-crystallin aggregate as is corroborated from the circular dichroism studies. The value of electrostatic interaction factor w which remains more or less constant between pH 4.6 and 9.25 is also found to gradually fall off below pH 4.6.
OBJECTIVE: To determine if the calculated anion gap differs according to presence or absence of hypertension in pregnant women. METHODS: Retrospective data were obtained for 1223 patients who delivered at a community hospital during a 6-month period. Fifty-six (4.6%) of these patients were considered to have proteinuric hypertension, 66 (5.4%) to have non-proteinuric hypertension, and 1101 (90%) to be normotensive. The Kruskal-Wallis and Mann-Whitney tests were used to compare these groups with respect to the anion gap and serum sodium, chloride, and bicarbonate. RESULTS: Compared with the other two groups, proteinuric hypertensive patients tended to have lower values for serum sodium (P < .005) and the anion gap (P < .005). There were no statistically significant differences between the groups with respect to serum chloride or bicarbonate. CONCLUSION: The anion gap appears to be smaller with proteinuric hypertension than it is without.