منابع مشابه
Spinal Chloroprocaine Solutions: Density at 37° C and pH Titration
The density and pH of a local anesthetic are important characteristics in its use as an intrathecal drug. Preservativeand antioxidant-free formulations of chloroprocaine are available and are being investigated for short-duration spinal anesthesia. In this study, we evaluated the pH and density (to 5 significant digits in g/mL, at 37.0°C) of these new chloroprocaine formulations. In addition to...
متن کاملAssay of carbonic anhydrase by titration at constant pH.
1. A method is described for measuring accurately the initial velocity of the hydration reaction catalysed by the enzyme carbonic anhydrase (EC 4.2.1.1); the method depends on the titration of H(+) ions at constant pH. 2. Human erythrocyte carbonic anhydrase, isoenzyme C, was used to illustrate the method. Under the experimental conditions employed (0 degrees , pH7.0, in the presence of 45mm-so...
متن کاملA novel view of pH titration in biomolecules.
When individual titratable sites in a molecule interact with each other, their pH titration can be considerably more complex than that of an independent site described by the classical Henderson-Hasselbalch equation. We propose a novel framework that decomposes any complex titration behavior into simple standard components. The approach maps the set of N interacting sites in the molecule onto a...
متن کاملConstant-pH molecular dynamics using continuous titration coordinates.
In this work, we explore the question of whether pK(a) calculations based on a microscopic description of the protein and a macroscopic description of the solvent can be implemented to examine conformationally dependent proton shifts in proteins. To this end, we introduce a new method for performing constant-pH molecular dynamics (PHMD) simulations utilizing the generalized Born implicit solven...
متن کاملpH titration of native and unfolded ß-trypsin: evaluation of the ∆∆G0 titration and the carboxyl pK values
The stabilizing free energy of ß-trypsin was determined by hydrogen ion titration. In the pH range from 3.0 to 7.0, the change in free energy difference for the stabilization of the native protein relative to the unfolded one (∆∆G0 titration) was 9.51 ± 0.06 kcal/mol. An isoelectric point of 10.0 was determined, allowing us to calculate the Tanford and Kirkwood electrostatic factor w. This fact...
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ژورنال
عنوان ژورنال: Journal of Chemical Education
سال: 2003
ISSN: 0021-9584,1938-1328
DOI: 10.1021/ed080p709.2