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Protein ovalbumin

Storage proteins Ovalbumin Casein Zein Phaseolin Eerritin... [Pg.121]

The surfactants associate at the oxide surface to form hemi-micelles with their hydrophobic groups exposed to the aqueous phase at low concentrations, but at higher concentrations, with the hydrophilic groups turned outwards. Hematite coated with various proteins (ovalbumin, y-globulin, lysozyme) adopted either the iep of the proteins or a value between that of the oxide and the protein and displayed modified coagulation behaviour (Johnson and Matijevic, 1992). [Pg.245]

The proteins ovalbumin (pH/= 4.6), urease (pH/=5.0), and myoglobin (pH/= 7.0) were applied to a column of DEAE-cellulose at pH 6.5. The column was eluted with a dilute pH 6.5 buffer, and then with the same buffer containing increasing concentrations of sodium chloride. In what order will the proteins be eluted from the column ... [Pg.102]

Pedron et al generated ABA-protein (ovalbumin or BSA) conjugates through the C-1 carboxyl group or the C-4 carbonyl group of ABA (11 and 12) [20]. ELISA detection showed that these ABA-protein conjugates bound efficiently to the solubilized microsomal protein fraction of Arabidopsis thaliana, independent of the nature of the carrier protein or the ABA-carrier protein linker. Purification of these binding proteins has not yet been reported. [Pg.331]

Source (L(-))-Phenylalanine is isolated commercially from proteins (ovalbumin, lactalbumin, zein, and fibrin). DL-Phenylalanine is synthesized from a-acetaminocinnamic acid. [Pg.972]

Fig. 3.7 KLKL5KLK induces antigen-specific humoral type 2 responses. The protein ovalbumin (OVA) was injected twice (on days 0 and 28) alone, or in combination with KLKL5KLK or alum. Serum samples were taken from mice at day 26 (prime) or day 54 (boost) and analyzed for IgGl by ELISA. Fig. 3.7 KLKL5KLK induces antigen-specific humoral type 2 responses. The protein ovalbumin (OVA) was injected twice (on days 0 and 28) alone, or in combination with KLKL5KLK or alum. Serum samples were taken from mice at day 26 (prime) or day 54 (boost) and analyzed for IgGl by ELISA.
The formulas show the a-carbon and the side chain of the amino acid residues, line phosphatase, phosphorylase kinase, glycogen synthetase, troponin, RNA polymerase, polynucleotide, phosphorylase, and triglyceride lipase. Phosphoserine is also found in nonenzyme proteins which include histones, protamiens, ribosomal proteins, membrane proteins, ovalbumin, casein, and phosvitin often in substantial amounts. For example, there are 119 phosphoserines and only one phosphothreonine residue in phosvitin (72). [Pg.119]

Specificity Ovalbumin and ovomucoid Egg white proteins Multiantigens (egg) Ovalbumin Egg white proteins (ovalbumin, ovomucoid, ovotransferrin, lysozyme) Egg white and yolk proteins Ovomucoid... [Pg.325]

Specificity Egg residue Whole egg proteins Ovalbumin Ovalbumin Ovomucoid Ovomucoid... [Pg.326]

Result reported as Egg residue Egg protein Egg protein Ovalbumin Ovomucoid Egg white protein... [Pg.326]

In our study we used four different glycoprotein acceptors which all have different numbers of carbohydrate acceptor sites per molecule of protein ovalbumin (0.9 mol of N-acetylglucosamine/mol protein), a... [Pg.84]

The amorphous hydrous oxide of Cr(III) (HCO) has been studied extensively as a source of sols of uniform particle size and shape [30] and as an electrophoresis standard [31] however, it has not been studied extensively as an adsorbent of metal ions. Sen [32] found that chromium (III) hydroxide generally has a larger adsorption capacity than the hydroxides of other triple-charged metals. Simon et al. [33] reported that coprecipitation of Cd(II) with chromium(III) hydroxide removed Cd(Il) from solution at a pH that was two units lower than that obtained using aluminum(III) hydroxide as the coprecipitating hydroxide. Similarly, Packter and Panesar [34] used Cr(III) and Mg(II) mixtures to show enhanced removal for both ions compared with the individual metal systems. HCO has also been used as an adsorbing surface to effectively adsorb the proteins ovalbumin, y-globulin, and lysozyme as a separation technique [351. [Pg.690]


See other pages where Protein ovalbumin is mentioned: [Pg.156]    [Pg.44]    [Pg.295]    [Pg.834]    [Pg.864]    [Pg.928]    [Pg.158]    [Pg.187]    [Pg.81]    [Pg.83]    [Pg.549]    [Pg.137]    [Pg.605]    [Pg.459]    [Pg.318]    [Pg.243]    [Pg.600]    [Pg.174]    [Pg.218]    [Pg.1435]    [Pg.167]    [Pg.62]    [Pg.928]    [Pg.2087]    [Pg.394]    [Pg.314]    [Pg.320]    [Pg.303]    [Pg.14]    [Pg.171]    [Pg.31]    [Pg.379]    [Pg.113]    [Pg.294]    [Pg.319]    [Pg.62]   
See also in sourсe #XX -- [ Pg.180 , Pg.338 ]




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Ovalbumin

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