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Albumin ovalbumin

Eier, n.pf. eggs, -albumin, n. egg albumin, ovalbumin, -dotter, m. yolk of eggs, -drtise, /. corpus luteum. -frucht,/. eggplant. gang, m. oviduct, -ol, n. egg-yolk oil, egg oil. -pulver, n. egg powder, custard powder, -schale, /. egg shell, -schalenglanz, m. eggshell luster. Stein, m. odlite, egg stone. [Pg.116]

Proteins. A chiral stationary phase with immobilized a -acid glycoprotein on silica beads was introduced by Hermansson in 1983 [18, 19]. Several other proteins such as chicken egg albumin (ovalbumin), human serum albumin, and cellohy-drolase were also used later for the preparation of commercial CSPs. Their selectivity is believed to occur as a result of excess of dispersive forces acting on the more retained enantiomer [17]. These separation media often exhibit only modest loading capacity. [Pg.58]

Douglas et al. [98] have measured protein (serum albumin, ovalbumin, and hemoglobin) mobilities over a range of pH values using a free-flow electrophoresis apparatus and a particle electrophoresis apparatus. They found good agreement between the two measurements however, they also found some differences between their measurements and those reported in the older literature. They attributed the differences to the use of moving-boundary electrophoresis methods in the early experimental work and to differences in... [Pg.588]

In fact, one finds from surface tension measurements that some proteins are considerably more hydrophobic (such as hemoglobin) than others (such as bovine serum albumin, ovalbumin). These properties of proteins have been extensively investigated. [Pg.43]

To become immunogenic, a hapten has to be linked with a large molecule, such as a protein, prior to its introduction into the host animal. Several proteins can act as such carrier molecules including bovine serum albumin, human serum albumin, ovalbumin, thyroglobulin, poly-L-lysine, and hemocyanin. Among these proteins, bovine serum albumin is most commonly used because it is inexpensive, readily available, very soluble, highly immunogenic, and, in addition, resists denaturatlon (3). [Pg.828]

Figure 3.9. SDS gel electrophoresis of MFGM proteins prepared by different washing procedures. S reference proteins phosphorylase B, bovine serum albumin, ovalbumin, carbonic anhydrase, trypsin inhibitor, a-lactal-bumin. (Courtesy of J. Basch and H. M. Farrell, Jr.)... Figure 3.9. SDS gel electrophoresis of MFGM proteins prepared by different washing procedures. S reference proteins phosphorylase B, bovine serum albumin, ovalbumin, carbonic anhydrase, trypsin inhibitor, a-lactal-bumin. (Courtesy of J. Basch and H. M. Farrell, Jr.)...
The most commonly biopolymers separated by Fl-FFF are proteins [49]. Fl-FFF is capable of separating proteins differing by just 15% in size within 3 to 10 min. S-Fl-FFF has been applied to a variety of proteins, including albumin, ovalbumin, y-globulin, hemoglobin, ferritin, lysozyme, [1-casein, apoferritin, human and rat blood plasmas and elastin [41,240,247]. Fl-FFF was also used to investigate the structural transformations of proteins [240]. [Pg.150]

Bovine serum albumin Ovalbumin Trypsin inhibitor ... [Pg.226]

Peters (1959) found, however, that decrease in absorbance at 280 m in urea with proteins (bovine and human serum albumins, ovalbumin, lysozyme) was not instantaneous, but required 20-60 min depending on the amount of NES added, while other spectral changes occurred within one minute (cf. Section V, B). [Pg.282]

Antibiotics, hormones, monoclonal antibodies, plasma proteins, insulin, vaccines, alkaloids Whey proteins, milk proteins, egg proteins, soy proteins, vitamins, amino acids, protein hydrolysates, yeast cells, yeast extract Glucose oxidase, peroxidase, hormones Detergent enzymes, insecticides Bovine serum albumin, ovalbumin, lysozyme Plant extracts, animal tissue extracts... [Pg.498]

The chemical score is determined as follows. The contents of the indispensable amino adds of egg albumin (ovalbumin), which is used as a reference protein, and the food protein in question arc determined. Egg albumin is considered to be ideal and nutritionally complete The test requires several steps. The protein must be purified, hydrolyzed to the constituent amino acids, and then subjected to analysis using an amino acid analyzer. The values for each of the indispensable amino acids for ovalbumin and the test protein are then listed as shown in Table 8.14. The contents of the various amino acids in the two proteins are then compared. The amino acid in the test protein that is present in the low cst level, on a percentage basis, can be found by examining the table. This amino acid is called the limiting amino acid of the protein. The value of the percentage is the chemical score. Table S.14 indicates that the quantity of lysine in oat protein is 51% that in egg protein. Hence, the chemical score of oat protein is 51,... [Pg.470]

Albumin ovalbumin carbonic anhydrase hemoglobin hexokinase MWCNTs MWCNT-COOH MWCNT-tyrosine MWCNT-isobutane amine CD Fluorescence The functionalized MWCNTs selectively induced protein secondary structure changes. Structural changes depend on the enzyme used and the functional group and the concentration of MWCNTs. [136]... [Pg.51]

The hydrogen ion usually is held so tightly by the anion portion that it is not eluted with water. This makes this resin excellent for the rapid quantitative removal of acids. Some other applications are the continuous separations of glucose-salt mixtures, sucrose from molasses, and sodium dodecyl sulfate from proteins (albumin, ovalbumin, cytochrome c) salt from blood, milk, and whey and kinins and amino acids from salts and buffers. [Pg.289]

Figure 7-5 The ionic strength dependence of the monomer/dimer equilibrium of P. denitrificans cytochrome C550- Cytochrome csso (2.3 nmol) dissolved in 10 mM Hepes, pH 8.0, containing the appropriate NaCl concentration, were passed down a Superdex 75 column equilibrated in the same buffer. The elution volume was compared with a set of standards (serum albumin, ovalbumin, carbonic anhy-drase, myoglobin and cytochrome c) in order to obtain a value of Mr. O, oxidized cytochrome C550 , cytochrome C550 reduced with 1 mM ascorbate. Figure 7-5 The ionic strength dependence of the monomer/dimer equilibrium of P. denitrificans cytochrome C550- Cytochrome csso (2.3 nmol) dissolved in 10 mM Hepes, pH 8.0, containing the appropriate NaCl concentration, were passed down a Superdex 75 column equilibrated in the same buffer. The elution volume was compared with a set of standards (serum albumin, ovalbumin, carbonic anhy-drase, myoglobin and cytochrome c) in order to obtain a value of Mr. O, oxidized cytochrome C550 , cytochrome C550 reduced with 1 mM ascorbate.
Ovalbumin, a member of the albumins. Ovalbumin is a glycoprotein (hen ovalbumin Mr 44.5 kDa 385 aa) characterized by four sites of post-translational modifications. Beside the acetylated N-terminus, the carbohydrate moiety is located at Asn , and the two phosphorylated serines at residues 68 and 344. Ovalbumin is a non-inhibitory member of the serine protease inhibitor family of the serpins. It has been classified as ovalbumin A1-A3, depending on the number of phosphorylated serine residues. Ovalbumin comprises 60% of the total protein amount of egg-white [A. D. Nisbet et al., Eur. J. Biochem. 1981, 115, 335 J. A. Huntington, P. E. Stein, J. Chromate. B 2001, 756, 189]. [Pg.254]

FIGURE 50.15 Fluorescent images of on-chip 2D separation of five model proteins using multiple separation media, (a) Non-native IFF with focusing order of (i) actin (ii) bovine serum albumin, ovalbumin, and trypsin inhibitor and (iii) parvalbumin from left to right (b) electrokinetic transfer of focused proteins (c) SDS-gel electrophoresis. (From Li et al.. Ana/. Chem., 76, 742, 2004. With permission.). [Pg.1390]

Such a "self-beating experiment on biologically interesting molecules was first published by Dubin et al. (14), who made measurements of bovine serum albumin, ovalbumin, lysozyme, and polystyrene latex spheres. They also studied tobacco mosaic virus and DNA and found that the nonsphericity of these molecules leads to deviations from the Lenentzian spectrum. A theoretica] analysis by Pecoia (IS), which predicts angular-dependent, multi-Lorentzian spectra, can be used to obtain shape information of such molecules. [Pg.612]

Fig. 1. Ultrogel AcA 54 chromatography of sARF I effect of dimyristoyl phosphatidylcholine (DMPC) on ADP-ribosylation of Gsa and choleragen A protein. Purified sARF I was chromatographed on a column (1.2 x 104 cm) of Ultrogel AcA 54. Fractions (1 ml) were collected and samples were (A) analyzed by sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and assayed for ARF activity in a reaction mixture containing Gg (0.4 jig), choleragen (25 pg), and 100 pM GTP without (B) or with (C) 1 mM DMPC. (A) SDS-PAGE of 250 pi of fraction plus bovine serum albumin, 10 pg. Lanes 1-4, fractions 68, 72, 76 and 80 Lane 5, standard proteins, phosphorylase b, bovine serum albumin, ovalbumin, carbonic anhydrase, soybean trypsin inhibitor, a-lactalbumin. (B) and (C) Autoradiograms of ADP-ribosylated proteins. Lanes 1-4, fractions 68,72,76 and 80 Lane 5, column buffer. Fig. 1. Ultrogel AcA 54 chromatography of sARF I effect of dimyristoyl phosphatidylcholine (DMPC) on ADP-ribosylation of Gsa and choleragen A protein. Purified sARF I was chromatographed on a column (1.2 x 104 cm) of Ultrogel AcA 54. Fractions (1 ml) were collected and samples were (A) analyzed by sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and assayed for ARF activity in a reaction mixture containing Gg (0.4 jig), choleragen (25 pg), and 100 pM GTP without (B) or with (C) 1 mM DMPC. (A) SDS-PAGE of 250 pi of fraction plus bovine serum albumin, 10 pg. Lanes 1-4, fractions 68, 72, 76 and 80 Lane 5, standard proteins, phosphorylase b, bovine serum albumin, ovalbumin, carbonic anhydrase, soybean trypsin inhibitor, a-lactalbumin. (B) and (C) Autoradiograms of ADP-ribosylated proteins. Lanes 1-4, fractions 68,72,76 and 80 Lane 5, column buffer.
Different formulations of saponin-adjuvanted vaccines were tested for humoral and cell-mediated responses in mice. Many antigens, often including hen egg albumin (ovalbumin, OVA) as the antigen to be tested, have been used for immunizations, enzyme immunoassays, antigen-specific CTL and cellular proliferation assays [31]. [Pg.252]

Digestion of bovine serum albumin, ovalbumin and dimethylcasein at various pH by acid protease from seminal plasma... [Pg.338]


See other pages where Albumin ovalbumin is mentioned: [Pg.135]    [Pg.67]    [Pg.21]    [Pg.325]    [Pg.325]    [Pg.185]    [Pg.78]    [Pg.171]    [Pg.256]    [Pg.54]    [Pg.502]    [Pg.502]    [Pg.513]    [Pg.135]    [Pg.546]    [Pg.198]    [Pg.331]    [Pg.143]    [Pg.135]    [Pg.245]    [Pg.370]    [Pg.612]    [Pg.487]    [Pg.514]    [Pg.432]    [Pg.235]    [Pg.432]    [Pg.338]   


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Ovalbumin

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