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Bovine y-globulin

Patients with protein-calorie malnutrition, especially children with marasmus and chest infections, had very high levels of serum IgD (R7). Antigen binding activity of IgD to diphtheria-toxoid and to bovine y-globulins in some human sera have been reported (G4, H3). [Pg.160]

Imanishi et al. [33] pointed out that there was an optimum point at which the tethering density of PEO chains makes a polybutadiene urethane surface biocompatible. They also reported that bovine plasma FGN and bovine y-globulin adsorbed on the PEO-modified polyurethane were completely denatured, in comparison with 4-38% denaturation of BSA adsorbed. [Pg.16]

Table 8-4. Affinities of Anti-DNP Antibodies Isolated at Varying Times After Injection of DNP-Bovine -y-Globulin... Table 8-4. Affinities of Anti-DNP Antibodies Isolated at Varying Times After Injection of DNP-Bovine -y-Globulin...
Fig. 2. The dependence of nucleoside-protein conjugation on pH. A mixture of periodate-oxidized adenosine and cytidine was added to bovine y-globulin to give final concentrations of 4 mM nucleoside (0.9 mg/ml) and 6.7 ftM protein (1 mg/ml) in 0.2 M Veronal buffer titrated to varying pH. These mixtures were incubated at room temperature for 1.5 hr. Then sodium borohydride was added to a final concentration of 0.4 M (15 mg/ml), and samples were incubated for 2.5 hr at 4°. They were then dialyzed extensively against 0.1 M NaCl and analyzed for protein and nucleoside composition. Fig. 2. The dependence of nucleoside-protein conjugation on pH. A mixture of periodate-oxidized adenosine and cytidine was added to bovine y-globulin to give final concentrations of 4 mM nucleoside (0.9 mg/ml) and 6.7 ftM protein (1 mg/ml) in 0.2 M Veronal buffer titrated to varying pH. These mixtures were incubated at room temperature for 1.5 hr. Then sodium borohydride was added to a final concentration of 0.4 M (15 mg/ml), and samples were incubated for 2.5 hr at 4°. They were then dialyzed extensively against 0.1 M NaCl and analyzed for protein and nucleoside composition.
The introduction of succinyl residues producing short-range repulsive forces in place of possible short-range attractive forces in the native molecule resulted in a change of hydrodynamic properties of bovine serum albumin (BSA), bovine y-globulin, and /3-lactoglobulin [3], The succinylated derivatives showed markedly increased intrinsic viscosity and Stokes radius and a decrease of sedimentation coefficient [36,37], These results are compatible only with a considerable increase in the effective volume occupied by the succinylated protein molecule compared to its unreacted counterpart. [Pg.66]

Figure 4. Bovine y-globulin on sintered Teflon (3 mg/dL solution critical-point dried, partial gold decoration technique). Key bar equals 0.11xm. Figure 4. Bovine y-globulin on sintered Teflon (3 mg/dL solution critical-point dried, partial gold decoration technique). Key bar equals 0.11xm.
Proteins were obtained from Miles Laboratories as bovine serum albumin (BSA) monomer standard Fraction V (81-028-1-P338) and bovine y-globulins Fraction II (82-041-2-1086). L-Tryptophan (Matheson Coleman Bell), 0.3 mg/mL in PBS, was used as an intrinsic fluorescence experimental reproducibility standard. [Pg.354]

Figure 7. Adsorption isotherm for bovine y-globulin on hydrophilic quartz... Figure 7. Adsorption isotherm for bovine y-globulin on hydrophilic quartz...
Figure 12. Fluroescence emission spectra for evanescent wave excited interfaciaF L-tryptophan (A)y adsorbed bovine y-globulin (B)y and adsorbed BSA (C). Figure 12. Fluroescence emission spectra for evanescent wave excited interfaciaF L-tryptophan (A)y adsorbed bovine y-globulin (B)y and adsorbed BSA (C).
In 1965, Johnson et al [14] showed histones could enhance the antibody response of mice to bovine y-globulin. Moroson [15] suggested some polycations had immune adjuvant properties in the non-specific rejection of experimental tumors in mice. In 1972, Gall et al reported that several synthetic polycations (Primafloc C-7, (poly-vinylimidazoline) C-5, and C-3) showed strong adjuvant activity with diphtheria and... [Pg.188]

The commonly used standard protein BSA is highly reactive in this dye binding assay. As a consequence the protein content of the samples is underestimated. This systematic error does not matter in comparative analyses but brings about wrong absolute values. It is recommended that bovine y-globulin be employed as a standard instead. [Pg.176]

Anti-PNP antibodies are produced by rabbits immunized with PNP20-bovine y-globulin and are purified from a 50% ammonium sulfate precipitate of serum by affinity chromatography on t-2,4 dinitrophenyllysine agarose with elution by 2,4-dinitrophenylglycine/ The preparation is dialyzed against 0.2 M sodium borate-0.15 M NaCl, pH 8.0, to remove hapten. [Pg.507]

The proportions of k and X chains may change during immunization. For example, anti-2,4-dinitrophenyl (anti-Dnp) antibodies synthesized by guinea pigs 2 weeks after immunization with a bovine y-globulin-Dnp conjugate contain over 99% k chains (9), and several strains of mice produce antibodies to a(l 3)dextran that are almost exclusively X (10), despite the paucity of X chains in normal mouse serum. [Pg.314]

In spite of similarities to other Igs, antibody activity in IgD has been difficult to demonstrate. Sera from some patients allergic to penicillin G contain IgD specific for the benzylpenicilloyl antigenic determinant . Antibody activity to diphtheria toxoid, bovine y-globulin and cell nuclei were also shown to be associated with IgD However, absorption of activity with... [Pg.38]

Streptococcal peptides Enantiomeric dipeptides, Tiy- Dy. Ala-Ala, Phe-Phe, Tyr-Tyr, Lys-Ala, Asp-Ala (synthesized) Bovine serum-albumin, bovine y-globulin, o-chyrootrypsin, cytochrome c, bemo obin, lysozyme, myoglobin, ovalbumin, ovomucoid, pepsin, ribonuclease, thyroglobulin, trypsin (SephadexG-100,G-200) Ornithine carbamoylphosphate transferase (Sephadex G-200, G-200 superfiiK)... [Pg.432]


See other pages where Bovine y-globulin is mentioned: [Pg.155]    [Pg.104]    [Pg.53]    [Pg.63]    [Pg.102]    [Pg.172]    [Pg.76]    [Pg.88]    [Pg.271]    [Pg.141]    [Pg.64]    [Pg.358]    [Pg.230]    [Pg.317]    [Pg.319]    [Pg.61]    [Pg.326]    [Pg.414]    [Pg.461]    [Pg.432]    [Pg.438]    [Pg.118]    [Pg.125]    [Pg.146]    [Pg.208]    [Pg.438]    [Pg.626]   
See also in sourсe #XX -- [ Pg.357 ]




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