zwitterion

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Related to Ampholytes: isoelectric point, zwitterion

zwitterion

[′tsfid·ər‚ī‚än]
(chemistry)
McGraw-Hill Dictionary of Scientific & Technical Terms, 6E, Copyright © 2003 by The McGraw-Hill Companies, Inc.
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Two-Dimensional Gel Electrophoresis (2DE): Anequivalent of 100 g of proteins in rehydration buffer [7M Urea, 2 M Thiourea, 50 mM DTT, 4% (w/v) CHAPS, and 0.4% (v/v) carrier ampholytes (pH 3-10, BioRad)] was loaded onto a 7 cm, pH 3-10 immobilised pH gradient strip (IPG, BioRad, USA).
It was established that synthesized ampholytes possess sufficient high sorption and complexing ability in relation to ions of copper, nickel, uranyl both from sour and alkaline solutions.
18 cm IPG strip pi 4-7 (Bio-Rad, Hercules, CA, USA) were rehydrated with the protein samples for 1 h at 4 C in a total volume of 350 [micro]l of rehydrating buffer (8 M urea, 2% CHAPS, 0.0007% of bromophenol blue, 18 mM DTT, 0.8% ampholytes of pH 3-10).
Briefly, up to 10 [micron]g of total protein was loaded onto each prefocused 7.5 cm x 25 mm (i.d.) tube gel containing 1.6% (w:v) ampholytes (pH 5-7) and 0.4 (w:v) ampholytes (pH 3.6-9.5), and proteins were separated by isoelectric focusing.
Although gel-based techniques for protein separation are tremendously powerful, the observation of protein bands reflects a complex set of interactions between protein, ampholytes, buffer composition, gel composition, and pore size.
Pellet was dried under reduced pressure and dissolved in 2D sample buffer containing 9.5M Urea, 4% NP-40, 5% (v/v) 2-mercaptoethanol, 2% v/v ampholytes of pH 5-8 and pH 3-10.
Protein solubilization is achieved utilizing chaotrops (urea), reducing agents (dithiothreitol), detergents (CHAPS, Triton-X), buffers (Tris), and <0.2% ampholytes. In addition, size, charge, and isoelectric point of proteins of interest are important characteristics for sample preparation.
Following the final wash step, the pellets, which contained the precipitated proteins, were vacuum-dried for 30 min and then were resolubilized with 0.5 mL rehydration/sample buffer which contained 8 M urea, 2% 3-[3-(cholamidopropyl)dimethylammonio]-1-propane sulfonate, 40 mM DTT, 0.2% Bio-Lyte 3/10 (ampholytes), and 2 mM tributylphosphine (TBP).
The focusing gels contained the following components: 4.3% total acrylamide with an acrylamide to bisacrylamide ratio of 37.5:1, 9 M urea, 2% ampholytes (pH range 3-10), and 1% Triton X-100.
Proteins are ampholytes, exhibiting amphoteric behavior owing to the presence of both positively- and negatively-charged side chain groups distributed along the length of the molecule and at its ends.
Isoelectric focusing was conducted on 0.25 mm polyacrylamide gels consisting of 2 ml 29.1 % (wt/vol) acrylamide and 0.9% N,N'-methy-lenebisacrylamide, 1.0 ml ampholytes (pH gradient 4-5; Crescent Chemical, Hauppa, NY), 4.2 ml deionized water, and 1.0 ml glycerol.