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Protein electrophoretic properties

Figure 3. Gel electrophoretic properties of glandless cottonseed proteins that are soluble at various suspension pH values... Figure 3. Gel electrophoretic properties of glandless cottonseed proteins that are soluble at various suspension pH values...
Figure 9. Gel electrophoretic properties of peanut meal proteins that are soluble in suspensions that contain various levels of salt and are at different pH values (25)... Figure 9. Gel electrophoretic properties of peanut meal proteins that are soluble in suspensions that contain various levels of salt and are at different pH values (25)...
Figure 13. Gel electrophoretic properties of soluble proteins in suspensions at various pH values that contain succinyl-ated liquid cyclone processed cottonseed flour... Figure 13. Gel electrophoretic properties of soluble proteins in suspensions at various pH values that contain succinyl-ated liquid cyclone processed cottonseed flour...
In the quantitative sections of this chapter the primary emphasis has been on establishing the relationship between the electrophoretic properties of the system and the zeta potential. We saw in Chapter 11 that potential is a particularly useful quantity for the characterization of lyophobic colloids. In this context, then, the f potential is a valuable property to measure for a lyophobic colloid. For lyophilic colloids such as proteins, on the other hand, the charge of the particle is a more useful way to describe the molecule. In this section we consider briefly what information may be obtained about the charge of a particle from electrophoresis measurements. [Pg.565]

Proteins are complex molecules, and classification has been based mostly on solubility in different solvents. Increasingly, however, as more knowledge about molecular composition and structure is obtained, other criteria are being used for classification. These include behavior in the ultracentrifuge and electrophoretic properties. Proteins are divided into the following main groups simple, conjugated, and derived proteins. [Pg.80]

McWatters and Cherry (9) characterized the emulsion and foam capacity, emulsion viscosity, protein solubility, and gel electrophoretic properties of water suspensions containing... [Pg.11]

Figure 8. Gel electrophoretic properties of peanut proteins as influenced by pH... Figure 8. Gel electrophoretic properties of peanut proteins as influenced by pH...
Figure 14. Gel electrophoretic properties of proteins in peanut flour treated with... Figure 14. Gel electrophoretic properties of proteins in peanut flour treated with...
Electrophoresis of a crystalline preparation revealed one major enzymatically active component and a minor inactive one (Negelein and Wulff, 1937). The smaller, inactive constituent varied from 5% to 20% of the total protein. Re-examination of the electrophoretic properties of yeast ADH crystals confirmed the presence of one slow, presumably active, and one fast-moving, presumably inactive component. Their relative amounts did not change systematically with recrystallization as shown by area analysis. The percentage of inactive component was a function of age of the solution and duration of preliminary dialysis. Preparations dialyzed for 20 hours at pH 5 contained as much as 14 % to 25 % of the inactive component, while dialysis for 4 hours showed as little as 6 %. The second component was assumed to be an inactive transformation product of the active enzyme (Hayes and Velick, 1954). [Pg.354]

Proteins can ba fractionated by electrophoretic techniques on the basis of one or a combination of their three major properties size, net charge and relative hydrophobicity. Electrophoresis under native conditions is ideal for soluble proteins, where biological properties can often be retained. In contrast, more vigorous and often denaturing conditions must be used for analysis of less soluble proteins. Electrophoretic separations can be carried out using either a continuous or discontinuous (Multiphasic) buffer system. The techniques are referred to as continuous zone electrophoresis (CZE) or discontinuous ("disc") electrophoresis (also known as multiphasic zone electrophoresis, MZE). [Pg.21]

Similar electrophoretic properties of subfractions have also been observed in the horse (51) and human (72) enzyme forms, but it seems that the rat alcohol dehydrogenase is most sensitive to conversions. This may be accounted for by the fact that the rat enzyme has the greatest total cysteine content (80,84) and, in particular, an extra cysteine residue at position 112 (Section II,B,3). This is close to the four cysteine residues which are ligands to the second zinc atom (Section II,C,3,b) and which are common to all three mammalian proteins (Section II,B). These residues are therefore in close proximity, compatible with formation of disulfide bridges without great structural or functional alterations. In addition, this region, from the tertiary structure (Section II,C,3,b), seems less essential for catalytic activity. [Pg.112]

Shea, T.B., Beermann, M.L. and Nixon, R.A. (1992) Aluminum alters the electrophoretic properties of neurofilament proteins role of phosphorylation state. J. Neurochem. 58 542-547. [Pg.504]

Santoni, V., S. Kieffer, D. Desclaux, F. Masson, and T. Rabilloud. 2000, Membrane proteomics use of additive main effects with multiplicative interaction model to classify plasma membrane proteins according to their solubility and electrophoretic properties. Electrophoresis 2 3329-3344. [Pg.52]

The results obtained with carbonmonoxyhemoglobins with and without dithionite ion in the buffers indicate that the dithionite ion plays no significant role in the electrophoretic properties of the proteins. It is therefore of interest that ferrohemoglobin was found to have a lower isoelectric point in phosphate buffer than carbonmonoxyhemoglobin. Titration studies have indicated (5, 6) that oxyhemoglobin (similar in electrophoretic properties to the carbonmonoxy compound) has a lower isoelectric point than ferrohemoglobin in... [Pg.414]

A reversible reaction catalyzes the conversion of pyruvate to phosphopyruvate, and the enzyme involved is pyruvic kinase. The equilibrium of that reaction is on the side of the formation of ATP. Thus, pyruvate kinase is the enzyme responsible for the conversion of phosphoenolpyruvate to pyruvate. The enzyme has been crystallized from muscle it requires ADP, potassium, and magnesium and is noncompetitively inhibited by some estrogenic steroids. Steroids alter the enzyme s viscosity and electrophoretic properties. From this observation, it was assumed that steroids act by modifying the protein molecule. [Pg.13]

LATS is believed to have a half-life of 20-30 days, a finding in keeping with the duration of the symptoms in neonatal hyperthyroidism. Available evidence suggests that LATS is a protein with a sedimentation constant of 7 and electrophoretic properties similar to those of globulin. LATS appears to be an immunoglobulin of the IgG type and possess the properties of an antibody. [Pg.456]

Two-dimensional polyacrylamide gel electrophoresis (2D PAGE) is a powerful approach to the analysis of complex protein mixtures as polypeptides are separated on the basis of two electrophoretic properties ... [Pg.283]

Multi-variable or cold-ethanol precipitation techniques yielded plasma protein fractions rich in lipoprotein (Oncley et al. 1949). These isolation procedures were extremely important. They demonstrated that physical properties such as solubility could be studied with lipoproteins as well as other proteins. Electrophoretic mobilities and specific refractive increments of lipoproteins were shown to be measurable properties (Armstrong et al. 1947 a and 1947 b). A detailed analysis of lipoprotein composition was undertaken (Oncley et al. 1950). [Pg.168]


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