Extraction and Separation of Water-Soluble Proteins from Different Wheat Species by Acidic Capillary Electrophoresis

2007 ◽  
Vol 55 (10) ◽  
pp. 3850-3856 ◽  
Author(s):  
Angela R. Piergiovanni
Keyword(s):  
Capillary Electrophoresis ◽  
Soluble Proteins ◽  
Water Soluble ◽  
Wheat Species ◽  
Extraction And Separation

scholarly journals Rapid separation and characterization of grain water-soluble proteins in bread wheat cultivars (Triticum aestivum L.) by capillary electrophoresis

2008 ◽  
Vol 88 (4) ◽  
pp. 843-848 ◽  
Author(s):  
Ai-li Wang ◽  
Yu-he Pei ◽  
Xiao-hui Li ◽  
Yan-zhen Zhang ◽  
Qian Zhang ◽  
...  
Keyword(s):  
Triticum Aestivum ◽  
Capillary Electrophoresis ◽  
Bread Wheat ◽  
Biochemical Markers ◽  
Soluble Proteins ◽  
Water Soluble ◽  
Wheat Cultivars ◽  
Organic Modifiers ◽  
Glycine Buffer

Water-soluble (WS) proteins in wheat grain are considered to represent the suite of biologically active enzymes and enzyme inhibitors in the grain. In this study, a rapid capillary electrophoresis (CE) method for WS protein separations was developed using untreated fused-silica columns and an acidic phosphate-glycine buffer system. In order to optimize the resolution and reproducibility of CE separation, different protein extraction methods, organic modifiers in phosphate-glycine buffer and capillary electrophoresis conditions, including capillary length and inner diameter (ID), operating temperature, performance voltages, sample injection times, etc., were investigated. High resolution and reproducibility of WS proteins were achieved using 20% ethanol as the extracting buffer. The optimal condition to separate these proteins was 50 μm ID × 31.5 cm (26.5 cm to the detector) capillary at 11.0 kV and 35°C. The optimum buffer was 0.1 M phosphate-glycine (pH 2.5) containing 20% acetonitrile (ACN) and 0.05% hydroxylpropylmethylcellulose. Using this method, the WS proteins were well separated in less than 10 min. A total of 120 Chinese bread wheat cultivars were analyzed. The CE patterns of most bread wheat cultivars showed a higher level of polymorphisms compared with SDS-PAGE patterns. All cultivars analyzed could be readily differentiated based on their WS protein profiles. Results indicate that the WS proteins are useful biochemical markers for wheat genetics and breeding research and CE is expected to become a new and powerful tool for the separation and characterization of grain WS proteins in bread wheat. Key words: Triticum aestivum, bread wheat, water-soluble proteins, capillary electrophoresis, biochemical markers

scholarly journals Chiral Selectors in Capillary Electrophoresis: Trends During 2017–2018

Molecules ◽  
2019 ◽  
Vol 24 (6) ◽  
pp. 1135 ◽  
Author(s):  
Raymond B. Yu ◽  
Joselito P. Quirino
Keyword(s):  
Capillary Electrophoresis ◽  
Molecular Mass ◽  
Chiral Separation ◽  
Chiral Separations ◽  
Water Soluble ◽  
Resonance Spectroscopy ◽  
Electrokinetic Chromatography ◽  
Chiral Selectors ◽  
Analytical Technique ◽  
Pharmaceutical Industries

Chiral separation is an important process in the chemical and pharmaceutical industries. From the analytical chemistry perspective, chiral separation is required for assessing the fit-for-purpose and the safety of chemical products. Capillary electrophoresis, in the electrokinetic chromatography mode is an established analytical technique for chiral separations. A water-soluble chiral selector is typically used. This review therefore examines the use of various chiral selectors in electrokinetic chromatography during 2017–2018. The chiral selectors were both low and high (macromolecules) molecular mass molecules as well as molecular aggregates (supramolecules). There were 58 papers found by search in Scopus, indicating continuous and active activity in this research area. The macromolecules were sugar-, amino acid-, and nucleic acid-based polymers. The supramolecules were bile salt micelles. The low molecular mass selectors were mainly ionic liquids and complexes with a central ion. A majority of the papers were on the use or preparation of sugar-based macromolecules, e.g., native or derivatised cyclodextrins. Studies to explain chiral recognition of macromolecular and supramolecular chiral selectors were mainly done by molecular modelling and nuclear magnetic resonance spectroscopy. Demonstrations were predominantly on drug analysis for the separation of racemates.

The cellular basis of corneal transparency: evidence for ‘corneal crystallins’

1999 ◽  
Vol 112 (5) ◽  
pp. 613-622 ◽  
Author(s):  
J.V. Jester ◽  
T. Moller-Pedersen ◽  
J. Huang ◽  
C.M. Sax ◽  
W.T. Kays ◽  
...  
Keyword(s):  
Cellular Level ◽  
Soluble Proteins ◽  
Water Soluble ◽  
Corneal Tissue ◽  
Corneal Epithelial Cells ◽  
Corneal Epithelial ◽  
Corneal Transparency ◽  
Scattering Measurements ◽  
Class 1

In vivo corneal light scattering measurements using a novel confocal microscope demonstrated greatly increased backscatter from corneal stromal fibrocytes (keratocytes) in opaque compared to transparent corneal tissue in both humans and rabbits. Additionally, two water-soluble proteins, transketolase (TKT) and aldehyde dehydrogenase class 1 (ALDH1), isolated from rabbit keratocytes showed unexpectedly abundant expression (approximately 30% of the soluble protein) in transparent corneas and markedly reduced levels in opaque scleral fibroblasts or keratocytes from hazy, freeze injured regions of the cornea. Together these data suggest that the relatively high expressions of TKT and ALDH1 contribute to corneal transparency in the rabbit at the cellular level, reminiscent of enzyme-crystallins in the lens. We also note that ALDH1 accumulates in the rabbit corneal epithelial cells, rather than ALDH3 as seen in other mammals, consistent with the taxon-specificity observed among lens enzyme-crystallins. Our results suggest that corneal cells, like lens cells, may preferentially express water-soluble proteins, often enzymes, for controlling their optical properties.

Selective Transport of Water-Soluble Proteins from Aqueous to Ionic Liquid Phase via a Temperature-Sensitive Phase Change of These Mixtures

2012 ◽  
Vol 65 (11) ◽  
pp. 1548 ◽  
Author(s):  
Yuki Kohno ◽  
Nobuhumi Nakamura ◽  
Hiroyuki Ohno
Keyword(s):  
Phase Change ◽  
Aqueous Phase ◽  
Selective Dissolution ◽  
Selective Extraction ◽  
Soluble Proteins ◽  
Water Soluble ◽  
Temperature Sensitive ◽  
Salting Out ◽  
Key Factor ◽  
The Difference

Mixtures of some ionic liquids (ILs) and water show reversible phase change between a homogeneous mixture and phase-separated state by a small change in temperature. Some water-soluble proteins have been migrated from the aqueous to the IL phase. When tetrabutylphosphonium 2,4,6-trimethylbenzenesulfonate was used as an IL, cytochrome c (Cyt.c) was found to be extracted from the water phase to the IL phase. Conversely, both horseradish peroxidase (HRP) and azurin remained in the aqueous phase. This selective extraction was comprehended to be due to the difference in solubility of these proteins in both phases. The separated aqueous phase contained a small amount of IL, which induced the salting-out of Cyt.c. On the other hand, condensed IL phase promoted the salting-in of Cyt.c. As a result, Cyt.c was preferably dissolved in the hydrated IL phase rather than aqueous phase. In the case of HRP, there was only a salting-out profile upon increasing the concentration of IL, which induced selective dissolution of HRP in the aqueous phase. These results clearly suggest that the profile of salting-out and salting-in for proteins is the key factor to facilitate the selective extraction of proteins from aqueous to the IL phase.

scholarly journals Influence of temperature processing on the constitutive and inducible resistance of rye seedlings to chloride salinization

2021 ◽  
pp. 134-140
Author(s):  
L. A. Chudinova ◽  
◽  
D. R. Yusupov ◽  
Keyword(s):  
Growth Rate ◽  
Sodium Chloride ◽  
Protective Effect ◽  
Soluble Proteins ◽  
Final Concentration ◽  
Water Soluble ◽  
Thermal Pretreatment ◽  
Thermal Hardening ◽  
Influence Of Temperature ◽  
Inducible Synthesis

We studied the growth rate of rye seedlings, as well as the dynamics of the content of soluble proteins and proline in the shoots during their adaptation to sharp (300 mM NaCl once, exposure time 9 days) and gradual (100 mM NaCl, then 100 mM NaCl after 2 days to the final concentration of 400 mM) salinity with sodium chloride in the presence or absence of thermal hardening (+40°C, 3 h). The established dy-namics of the content of proline and soluble proteins in the shoots suggests that the formation of re-sistance to salinity is determined by the high constitutive level of proline, as well as the stress-inducible synthesis of proline and water-soluble proteins. Thermal pretreatment of the seedlings stimulated their constitutive stability to a greater extent. The detected metabolic changes are obviously related to one of the possible mechanisms of the protective effect of thermal hardening on subsequent salinization.

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