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At least 343 records · Page 19Linked to original sources
PubMed1996

Intravenous calcium chloride in the conversion of paroxysmal supraventricular tachycardia to normal sinus rhythm.

This brief report describes several cases of paroxysmal supraventricular tachycardia that converted promptly to normal sinus rhythm within 1 to 2 minutes of receiving intravenous calcium salts as pretreatment in anticipation of verapamil therapy. A review of calcium's hemodynamic and dromotropic effects suggests that this probably was due to electrophysiological effects rather than mere coincidence. Calcium raises blood pressure, which may reflexively increase cardiac parasympathetic tone, and also has a direct slowing effect on atrioventricular conduction. Adenosine remains the drug of choice in the treatment of paroxysmal supraventricular tachycardia. However, in addition to preventing hypotension when used as pretreatment to verapamil, intravenous calcium itself may terminate supraventricular tachycardia.

Adult↗
PubMed1988

Parameters involved in binding of porcine pancreatic alpha-amylase with black bean inhibitor: role of sulfhydryl groups, chloride, calcium, solvent composition and temperature.

The amylase inhibitor of black (kidney) beans (Phaseolus vulgaris; MW 53,000) forms a 1:1 stoichiometric complex with porcine pancreatic alpha-amylase (MW 52,000) at pH 5.40. The single sulfhydryl group of the inhibitor and the two sulfhydryl groups of alpha-amylase are not involved in recognition and binding. Chloride ions, required for activity of alpha-amylase at both pH 5.40 and 6.90, are important for inhibitor--enzyme binding at pH 6.90 but not at pH 5.40. Calcium-free alpha-amylase binds with the inhibitor. An increase in the ionic strength of the solvent increases the rate of binding of the inhibitor with alpha-amylase; a decrease in the dielectric constant decreases the rate of binding; and decreasing the temperature increases the dissociation constant, Kd, of the complex. These data support the hypothesis that hydrophobic interaction is of primary importance in complex formation. The activation energy, Ea, for complex formation was found to be 12.4 kcal/mol at pH 5.40 and 24.2 kcal/mol at pH 6.90. In the presence of the poor substrate, p-nitrophenyl-alpha-D-maltoside, the Ea for complex formation was 4.1 kcal/mol at pH 6.90.

Animals↗
PubMed1975

The thermochemistry of reactions between alpha-s1-casein and calcium chloride.

The enthalpies of reactions between alpha-s1-casein and Ca2+ in solution were measured using a gradient layer calorimeter. The reactions are exothermic between 0 and 4.3 mM CaCl2. In the region of 4.3 mM CaCl2 there is a change to an endothermic reaction corresponding to micellisation. A calcium-binding curve has been obtained under the same conditions as the calorimetry experiments and this shows two sigmoidal binding phases. Turbidity measurements show that there is an association process corresponding to the second sigmoidal phase. A tentative interpretation of the heat curve in the region before micellisation is given in terms of the site binding of Ca2+, conformational changes in the protein and association. The main thermal processes are taken to be exothermic intramolecular hydrogen bonding induced by calcium binding and endothermic hydrophobic bonding.

Binding Sites↗