Ovalbumin solutions

Fig. 1.51. Unfreezable water (UFW) in a 0.57 % ovalbumin solution as a function of the freezing temperature with different CPAs (Fig. 4. from [1.36]).

The liberation of sulfhydryl groups was not detected after irradiation of 0.5% ovalbumin solutions. Since it was shown that the presence of inert protein protected, rather than inactivated, phenolase, it was concluded that thiol groups, produced by disruption of disulfide bonds in the protein, had no significant role in phenolase inactivation. 

In 1996, Gauglitz and coworkers coated surfaces with various amino-and carboxy-substituted polymers [198], The polymers tested were branched poly-(ethyleneimine), a,co-amino-functionalized PEG, chitosan, poly(acrylamide-co-acrylic acid) and an amino-modified dextran. The amino-substituted polymers were immobilized on glass by first immobilizing an aminosilane, followed by succinic anhydride/A-hydroxysuccinimide linker chemistry. Poly(acrylamide-co-acrylic acid) was directly coupled to an aminosilanized surface. When probed with 1 mg mL 1 ovalbumin solution, nonspecific adsorption was lowest for the dextran derivative. Notably, nonspecific adsorption increased in most cases when a hydrophobic hapten (atrazine) was coupled to the polymer-modified surface. 

Cells are often adsorbed on slides coated with ovalbumine or poly-L-lysine (Farr and Nakane, 1981). The ovalbumine solution is prepared by mixing one egg white with 1 ml of concentrated NH4OH and 500 ml distilled water, stirring for 10 min and filtering through several layers of gauze. The clean slides are placed for 1 min in this solution, excess is drained off and the slides are air-dried at room temperature (if relative humidity is low) or at higher temperatures (up to 60 C) for 2-18 h. These slides can be stored indefinitely. 

Photchanachai S, Mehta S, Kitabatake N (2000). Heating of an ovalbumin solution at neutral pH and high temperature. Biosci. Biotechnol Biochem., 66 1635-1640. 

Other studies included the investigation of the stabilizing effect of sorbitol on hen egg white lysozyme and the use of the self-diffusion coefficient, D, to follow the solution and aggregative properties of lysozyme at different pH, temperature, and protein and salt concentrations. The properties of frozen ovalbumin solutions were studied by NMR relaxation spectroscopy. It is known that the functional properties of muscle proteins are affected by protein interactions with ions, and NMR was used to assess protein/water, protein/salt, and protein/protein interactions in myofibrillar protein solutions. Previous X-ray and NMR studies on collagen and peptides were reviewed by Mayo and, more recently, such types of system were characterized by high-resolution H and C NMR. °0 The structure, hydration state, and nature of the interactions between water and gelatin were determined by time domain NMR. ... 

A. V. Guntelberg and K. Linderstrom-Lang, Osmotic Pressure of Plakalbumin and Ovalbumin Solutions, C. r. Trav. Lab. Carlsberg 27, 1-25 (1949). 

When a solution of ovalbumin is added to rabbit anti-ovalbumin serum (obtained from a rabbit that had been injected with ovalbumin) a precipitate forms. When more ovalbumin solution is added the precipitate dissolves. Can you explain these facts ... 

Albumins. Soluble proteins both in water and in dilute aqueous salt solutions found in all living tissue. Typical albumins are ovalbumin from eggs and lactalbumin from milk. 

The elution volume, F/, and therefore the partition coefficient, is a function of the size of solute molecule, ie, hydrodynamic radius, and the porosity characteristics of the size-exclusion media. A protein of higher molecular weight is not necessarily larger than one of lower molecular weight. The hydrodynamic radii can be similar, as shown in Table 4 for ovalbumin and a-lactalbumin. The molecular weights of these proteins differ by 317% their radii differ by only 121% (53). 

Monkos, Karol 2000. Viscosity analysis of the temperature dependence of the solution conformation of ovalbumin. Biophysical Chemistry 85, 7-16. 

Capsules were equilibrated with a tracer solution overnight. A capsule pellet (0.2-0.5 ml) was then placed in 5 ml test buffer (PBS or RPMI-1640 medium, Gib-co/BRL, New York, NY) on a shaker and a 0.2-ml aliquot was immediately sampled by a screen-protected pipette with further samples being taken over the next 700 s. The tracer quantity was assayed using the methods described below. A final sample was taken after the capsules has been in contact with the buffer for several hours (equilibrated tracer quantity) and the increment to the tracer concentration at each time was calculated. From the progress of tracer to equilibrium on a semilog plot a slope denoted as the zero -order rate flux constant was obtained and has been used as a measure of capsule permeability. [3H] -Glucose (580 daltons),insulin (6.2 kDa), and ovalbumin (45 kDa) have been used as tracers. Radioactivity was measured by means of a Packard 2000CA Liquid Scintillation Counter (Packard Instruments,... 

Hanafusa [1.36] showed with this method, how the amount of unfrozen water in a 0.57 % solution of ovalbumin reaches practically zero at -20 °C, if 0.01 M sucrose is added (Fig. 1.51). For globular proteins Hanafusa described the freezing process as follows between 0 °C and -20 °C, water molecules from the multilayer hydrate shell are decomposed. Be-... 

Fig. 1.52. Schematic model of CPA action in protein solutions during freezing and freeze drying. (Fig. 10 from [1.36]). Top row Without CPA the hydrate water of the ovalbumin has migrated into the ice and the freed valences are exposed to the influence of the environment. Second row With CPA a part of the hydrate water of the proteins becomes replaced by CPA molecules. These, together with the remaining water molecules and the protein molecule, form a quasi (replacement) hydrate layer.

Dissolve 4 mg of carrier protein (KLH, ovalbumin, BSA or the like) in about 400 pi of Soln. A. Add a solution of 4 mg peptide in 400 pi Soln. A and mix well. The molar ratio should be at least 10 moles of peptide per mole carrier protein. 

As a variant, activate the peptide separately first and couple then to the carrier Dissolve the peptide to 1 mg/ml in ddH20, add 10 mg EDAC hydrochloride per milligram of peptide, and adjust pH to 5.0. Incubate at RT for 5 min and correct the pH with diluted NaOH during this period. Then add the same volume of carrier protein solution. The amount of carrier protein should be in a ratio of 40 moles of COOH groups per mol peptide (ovalbumin 42.7 kD, 31 Asp, 48 Glu/Mole BSA 67.7 kD, 54 Asp, 97 Glu/Mole). Shake at RT for 4 h and stop the reaction by addition of 1/10 volume of 1 M sodium acetate buffer, pH 4.2. Free the sample from surplus reagents by gel filtration or dialysis and concentrate to about 1 ml by ultrafiltration. 

Immunostimulant activity. Fresh plant juice, in the ration of female mice, was active in ovalbumin-sensitized mice . Water extract of the dried root, taken orally by human adults, was active. A pharmaceutical solution containing fruit bodies of Tremella fuciformis, Daucus carom root, Astragalus mongholicus root and Zizyphus jujuba fruits, honey, vitamin A palmitate, zinc sulfate, and vitamin C is claimed useful as an immunostimulant for controlling AIDS, cancer, and infections L Inotropic effect (negative). Ethanol (80%) extract of the aerial parts, at a concentration of 0.3 mg/mL, was active on the guinea pig atrium . 

In contrast, the whey proteins are relatively small globular proteins. a-Lactalbumin represents about 20 % of the protein content of bovine whey (3.5 % of total bovine milk protein), and it is the principal protein in human milk (Brew and Grobler, 1992). Nanotube assembly has been discovered in some solutions containing a hydrolysed derivative of this protein. And it appears that the a-lactalbumin nanotube is unique in the sense that it is the only artificial nanotube that has so far been made from a food protein (Graveland-Bikker et al., 2004 Graveland-Bikker and de Kruif, 2006). As for p-lactoglobulin, it has the capacity under certain specific conditions to form nano-fibres in aqueous media (as can various other globular food proteins, such as ovalbumin, soy proteins, and bovine serum albumin) (van der Linden, 2006 Nicolai, 2007). 

Antipova, A.S., Semenova, M.G., Belyakova, L.E. (1999). Effect of sucrose on the thermodynamic properties of ovalbumin and sodium caseinate in bulk solution and at air-water interface. Colloids and Surfaces B Biointerfaces, 12, 261-270. 

Figure 14.7 Hs/2rQ plotted against 2rQ u/D g. fg 17-37 rm solute myoglobin, ovalbumin, bovine serum albumin. Temperature 10, 20, 40 °C.

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