The Solubility of Glutamic Acid in Water and Certain Organic Solvents

Pertzoff, Vladimir

doi:10.1016/s0021-9258(18)75985-1

Cited by 11 publications

(4 citation statements)

References 6 publications

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“…The high EC 50 value is problematic for measuring loss-of-function mutations for many reasons. Glutamate is not soluble at concentrations higher than 50 mM in buffered solution, and while a hydrochloride salt increases this solubility, it also dramatically increases the osmolarity of the solution to several times that of frog Ringer solution . Also, at high concentrations of glutamate, currents are observed in uninjected oocytes, which may be due to nonspecific activation of endogenous receptors or osmotic response.…”

Section: Resultsmentioning

confidence: 99%

Functional Evaluation of Key Interactions Evident in the Structure of the Eukaryotic Cys-Loop Receptor GluCl

2014

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The publication of the first high-resolution crystal structure of a eukaryotic Cys-loop receptor, GluClα, has provided valuable structural information on this important class of ligand-gated ion channels (LGIC). However, limited functional data exist for the GluCl receptors. Before applying the structural insights from GluCl to mammalian Cys-loop receptors such as nicotinic acetylcholine and GABA receptors, it is important to ensure that established functional features of mammalian Cys-loop receptors are present in the more distantly related GluCl receptors. Here, we seek to identify ligand-binding interactions that are generally associated with Cys-loop receptors, including the frequently observed cation−π interaction. Our studies were performed on the highly homologous GluClβ receptor, because GluClα is not activated by glutamate in Xenopus laevis oocytes. Mutagenesis of the signal peptide and pore lining helix was performed to enhance functional expression and sensitivity to applied ligand, respectively. Conventional and unnatural amino acid mutagenesis indicate a strong cation−π interaction between Y206 and the protonated amine of glutamate, as well as other important ionic and hydrogen bond interactions between the ligand and the binding site, consistent with the crystal structure.

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Section: Resultsmentioning

confidence: 99%

Functional Evaluation of Key Interactions Evident in the Structure of the Eukaryotic Cys-Loop Receptor GluCl

2014

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“…For molecules with solubility proportional to temperature, the enthalpy (ΔH) of solubilization is positive and the reaction is endothermic (Pertzoff, 1933). Although solubility data for βCPP have not been reported, comparison with glutamic acid (a reasonable proxy given that there are 7 in βCPP) shows that its solubility is proportional to temperature in both water and acetone (Pertzoff, 1933). The use of cold acetone improved precipitation of βCPP (Supplemental Table S1; http://dx.doi.org/10.3168/ jds.2016-11010).…”

Section: Resultsmentioning

confidence: 99%

Purification and identification of β-casein phosphopeptide (1-25)

Naqvi

Singh

Han

et al. 2016

Journal of Dairy Science

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The β-casein phosphopeptide 1-25 (βCPP) is involved in calcium binding, cellular transduction, and dental remineralization. The objective of this work was to improve upon the original protocol commonly used for isolation of this phosphopeptide from β-casein. This method exploits the isoelectric point of β-casein fragments to selectively precipitate βCPP. The highest βCPP extraction yield reported to date with this protocol is 14.4±0.5% of theoretically available βCPP. The present work optimizes 2 steps in this procedure, namely the length of trypsin digestion and incorporation of cold acetone precipitation, to increase the yield to 32.3±5.4%. Reverse-phase HPLC indicated high purity of the isolate, whereas mass spectrometry confirmed 2 forms of the phosphopeptide: fragments 1-25 (87%) and 2-25 (13%). The adaptation of the existing protocol represents a significant improvement in extraction yield and facilitates preparation of larger amounts of high-purity βCPP for subsequent analysis and use in functional foods and other applications.

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“…The experiments were performed by mixing the Glu-PEI aqueous solution with EtOH, which is a non-solvent for Glu (At 25 1C, Glu solubility is 0.11 mol% in pure water and 8.3 Â 10 À4 mol% in EtOH). 35 Without PEI, Glu is known to precipitate into single crystalline sheets directly from the water-EtOH mixture. 36 However, the existence of PEI can protect Glu from immediate precipitation and different Glu/PEI ratios can result in different phase behaviors of the quaternary system.…”

Section: Resultsmentioning

confidence: 99%

The existence region and composition of a polymer-induced liquid precursor phase for dl-glutamic acid crystals

Jiang

Gower

Volkmer

et al. 2012

Phys. Chem. Chem. Phys.

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The existence region of a polymer-induced liquid precursor (PILP) phase for crystals of an organic compound (DL-glutamic acid, Glu) was determined for the first time in the phase diagram of the Glu-polyethyleneimine-water-ethanol system. The existence region and the amount of PILP phase relative to the thermodynamically stable crystal phase were very small. Other phases detected in the phase diagram were coacervates, homogenous mixtures, and crystals obtained via a clear solution. The PILP phase is rich in the polymeric additive, which helps to explain the long induction period of PILP before crystallization occurs. Volume measurements indicated that its amount is <<1 vol%, showing that this precursor phase is only a minor component.

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The Solubility of Glutamic Acid in Water and Certain Organic Solvents

Cited by 11 publications

References 6 publications

Functional Evaluation of Key Interactions Evident in the Structure of the Eukaryotic Cys-Loop Receptor GluCl

Functional Evaluation of Key Interactions Evident in the Structure of the Eukaryotic Cys-Loop Receptor GluCl

Purification and identification of β-casein phosphopeptide (1-25)

The existence region and composition of a polymer-induced liquid precursor phase for dl-glutamic acid crystals

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