The Isoelectric Point

The swelling of gels is markedly affected by the presence of electrolytes, this effect being a minimum at the isoelectric point of the material. In general, sulphates, tartrates, etc. inhibit swelling, while iodides and thiocyanates promote the swelling. Thus gelatine disperses completely in iodide solution even at low temperatures. 

Figure V-8 illustrates that there can be a pH of zero potential interpreted as the point of zero charge at the shear plane this is called the isoelectric point (iep). Because of specific ion and Stem layer adsorption, the iep is not necessarily the point of zero surface charge (pzc) at the particle surface. An example of this occurs in a recent study of zircon (ZrSi04), where the pzc measured by titration of natural zircon is 5.9 0.1...

One potentially powerfiil approach to chemical imaging of oxides is to capitalize on the tip-surface interactions caused by the surface charge induced under electrolyte solutions [189]. The sign and the amount of the charge induced on, for example, an oxide surface under an aqueous solution is detenuined by the pH and ionic strength of the solution, as well as by the isoelectric point (lEP) of the sample. At pH values above the lEP, the charge is negative below this value. 

Table 27 2 includes a column labeled pi which is the isoelectric point of the ammo acid The isoelectric point, also called the isoionic point, is the pH at which the ammo acid has no net charge It is the pH at which the concentration of the zwitterion is a maximum At a pH lower than pi the ammo acid is positively charged at a pH higher than pi the ammo acid is negatively charged For the ammo acids m Table 27 2 pi is the average of pA i and pK 2 and lies slightly to the acid side of neutrality... 

Some ammo acids have side chains that bear acidic or basic groups As Table 27 3 indicates these ammo acids are characterized by three values The third pK reflects the nature of the side chain Acidic ammo acids (aspartic and glutamic acid) have acidic side chains basic ammo acids (lysine arginine and histidine) have basic side chains The isoelectric points of the ammo acids m Table 27 3 are midway between the pK values of the zwitterion and its conjugate acid Take two examples aspartic acid and lysine Aspartic acid has an acidic side chain and a pi of 2 77 Lysine has a basic side chain and a pi of 9 74... 

Thus if a mixture containing alanine aspartic acid and lysine is subjected to electrophoresis m a buffer that matches the isoelectric point of alanine (pH 6 0) aspartic acid (pi = 2 8) migrates toward the positive electrode alanine remains at the origin and lysine (pi =9 7) migrates toward the negative elec trode (Figure 27 3b)... 

FIGURE 27 3 Application of electrophoresis to the separation of aspartic acid alanine and lysine according to their charge type at a pH corresponding to the isoelectric point (pi) of alanine... 

The most stable structure of a neutral ammo acid is a zwitterion The pH of an aqueous solution at which the concentration of the zwitterion IS a maximum is called the isoelectric point (pi)... 

Isobutyl group (Section 2 13) The group (CH3)2CHCH2— Isoelectric point (Section 27 3) pH at which the concentration of the zwittenonic form of an amino acid is a maximum At a pH below the isoelectric point the dominant species is a cation At higher pH an anion predominates At the isoelec tnc point the ammo acid has no net charge Isolated diene (Section 10 5) Diene of the type... 

This table lists the and pi (pH at the isoelectric point) values of a-amino acids commonly found in proteins along with their abbreviations. The dissociation constants refer to aqueous solutions at 25°C. 

Sodium Poly(4-styrene sulfonate). The sol—gel processing of TMOS in the presence of sodium poly-4-styrene sulfonate (NaPSS) has been used to synthesize inorganic—organic amorphous complexes (61). These sodium siUcate materials were then isotherm ally crystallized. The processing pH, with respect to the isoelectric point of amorphous siUca, was shown to influence the morphology of the initial gel stmctures. Using x-ray diffraction, the crystallization temperatures were monitored and were found to depend on these initial microstmctures. This was explained in terms of the electrostatic interaction between the evolving siUcate stmctures and the NaPSS prior to heat treatment at elevated temperatures. 

Purified hGH is a white amorphous powder in its lyophilized form. It is readily soluble (concentrations >10 mg/mL) in dilute aqueous buffers at pH values above 7.2. The isoelectric point is 5.2 (3) and the generally accepted value for the extinction coefficient at 280 nm is 17,700 (Af-cm) (4),... 

A large part of the dissolved amino acid exists as the ampholyte (2witterion). The isoelectric point (pi) is the pH at which the net electric charge of a dissolved amino acid molecule is 2ero. p /is expressed as... 

Properties and Structure. a -Acid glycoprotein (a -AGP) has a molecular mass of about 41,000 and consists of a peptide chain having 181 amino acid residues and five carbohydrate units (14,15). Two cystine disulfide cross-linkages connect residues 5 and 147 and residues 72 and 164. The carbohydrate units comprise 45% of the molecule and contain siaUc acid, hexosamine, and neutral hexoses. In phosphate buffer the isoelectric point of the... 

As the pH is iacreased or decreased from the isoelectric point, the particles acquire a charge (surface potential) that can enhance repulsion. Surface charge on the particle can be approximated by measuring 2eta potential, which is the electrostatic potential at the Stem layer surrounding a particle. The Stem layer is the thickness of the rigid or nondiffiise layer of counterions at a distance (5) from the particle surface, which corresponds to the electrostatic potential at the surface divided by e (2.718...). 

It was noted that the content of functional groups on the surface of studied A1,03 was 0,92-10 mol/g of acid character for (I), FOS-IO mol/g of basic character for (II). The total content of the groups of both types was 1,70-lO mol/g for (III). The absence of appreciable point deviations from a flat area of titration curves in all cases proves simultaneously charges neutralization character on the same adsoi ption centers and non-depending on their density. The isoelectric points of oxide surfaces have been detenuined from titration curves and have been confirmed by drift method. 

Human serum albumin has been purified similarly with 25% EtOH and 0.2% decanol. The isoelectric points of bovine and human serum albumins are 5.1 and 4.9. 

At the pH = Jt there is a balance of charge and there is no migration in an electric field. This is referred to as the isoelectric point and is determined by the relative dissociation constants of the acidic and basic side groups and does not necessarily correspond to neutrality on the pH scale. The isoelectric point for casein is about pH = 4.6 and at this point colloidal stability is at a minimum. This fact is utilised in the acid coagulation techniques for separating casein from skimmed milk. 

Addition of acetic or mineral acid to skimmed milk to reduce the pH value to 4.6, the isoelectric point, will cause the casein to precipitate. As calcium salts have a buffer action on the pH, somewhat more than the theoretical amount of acid must be used. Lactic acid produced in the process of milk souring by fermentation of the lactoses present by the bacterium Streptococcus lactis will lead to a similar precipitation. 

The isoelectric points of the amino acids in Table 27.3 are midway between the pK values of the zwitterion and its conjugate acid. Take two exanples aspartic acid and lysine. Aspartic acid has an acidic side chain and a pi of 2.77. Lysine has a basic side chain and a pi of 9.74. 

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