Bovine serum albumin data

Figure 2 Examples of free energy change variation as a function of temperature for some examples of globular proteins. (Thermodynamic data obtained by DSC.) ALA (pH 6.5) a-lactalbumin at pH 6.5. (Data from Ref. 190.) BLG (pH 2) /3-Iactoglobulin at pH 2. (Data from Ref. 28.) BLG (pH 3.5) /3-laetoglobulin at pH 3.5. (Data from Ref. 45.) BSA (pH 7) bovin serum albumin. (Data from Ref. 64.)...

Figure 34 Effective cell partition coefficient of PNU-78,517 as a function of bovine serum albumin concentration. The inset shows the relationship between the effective permeability coefficient (Pe) of appearance and BSA concentration or the fraction of free drug. These data were obtained from the uptake data shown in Figure 33. [Redrawn from Raub et al. (1993) with permission from the publisher.]...

Recent data indicate that SR-BI is a nonspecific receptor for many lipophilic molecules (Lorenzi et al., 2008 Reboul et al., 2007b). Apart from HDLs, rodent SR-BI also binds to LDL, VLDL, acetylated LDL, oxidized LDL, and maleylated bovine serum albumin. SR-BII has a similar ligand specificity and function to that of SR-BI (Webb et al., 1998). However, it has been shown that vitamin E (which like carotenoids is carried in the bloodstream mainly by LDL and HDL) is transported more efficiently into the endothelial cells from HDLs than from LDLs (Balazs et al., 2004 Kaempf-Rotzoll et al., 2003 Mardones and Rigotti, 2004). This is in striking contrast to cholesterol, which is taken up much more efficiently from LDLs than HDLs by the RPE to the retina (Tserentsoodol et al., 2006b). It remains to be shown which lipoproteins are the main carriers for carotenoids transported from blood into the RPE. 

Fig. 44. LS plots142) for bovine serum albumin in iso-ionic salt free aqueous solution [plot (b)]. Also shown are data (open circles) for solution in 0.001 M NaCl [plot (c). Plot (a) is for same data as in (b) plotted against the square root of the bovine serum albumin concentration, c2, according to Eq. (94)...

Although the occurrence of six conserved cysteine residues, the spacing patterns of these residues, and possibly the pattern of disulfide structures are hallmarks of OBPs, the six-cysteine criterion alone is not sufficient to classify a certain protein as an olfactory protein [ 16]. It is important to demonstrate that an OBP is expressed only (or predominantly) in olfactory tissues. Evidence for their ability to bind odorants is also desirable, but not sine qua non. One of these criteria alone would not be enough to define a given protein as an OBP. For example, bovine serum albumin (BSA) binds to insect pheromones (Leal, unpublished data) and yet it is not an OBP because it not expressed in insect olfactory tissues. Conversely, a protein specific to antennae is not necessarily an OBP. There are other proteins that may be expressed in antennae but not in control tissues. Non-OBPs specifically accumulated in insect antennae have been previously detected (Ishida and Leal, unpublished data). Also, a glu-tathione-S-transferase has been reported to be expressed specifically in antennae of M. sexta [52]. 

Fig. 17. The water proton spin-lattice relaxation rates as a function of magnetic field strength reported as the proton Larmor frequency in aqueous 1.8 mM samples of bovine serum albumin. The lower data set was taken on the solution, the open circles taken after the sample had been cross-linked with glutaraldehyde to stop rotational motion (89).

EXAMPLE 3.5 Evaluation of Charges of Macroions from Osmotic Pressures. In Example 3.3, we evaluated M and B for bovine serum albumin at pH = 5.37, at which the molecule is known to be uncharged. Use the data in Figure 3.6 to evaluate B and, from it, the charge of the molecule at pH = 7.00. The data in Figure 3.6 were measured in 0.15 M NaCI. 

Solutions of bovine serum albumin in 0.15 M NaCl were studied at other pH levels in addition to those shown in Figure 3.6. The following data are examples of additional measurements ... 

The osmotic pressure of salt-free (electrodialyzed) bovine serum albumin solutions was measured at pH = 5.37 ( ). At this pH the net charge of the protein molecules is zero. The following data were obtained in different runs ... 

Serum albumin circulates in the blood stream transporting essential nutrients such as fatty acids to peripheral tissue. Transported molecules, called ligands, often have a special affinity for selected binding sites on proteins and nucleic acids. In this experiment, the dynamics of ligand-protein interactions will be explored with the binding of the dye phenol red to bovine serum albumin. The technique of gel filtration will be used to separate the dye-protein complex. Data will be analyzed in order to construct binding curves. 

Describe the color of the reaction mixtures just before loading onto the column. Make observations about the column development process. Analyze the absorbance data by preparing an elution curve. On graph paper or a computer graphics program, plot 520 (j-axis) versus fraction number. How many peaks were obtained What are the components represented by each peak Use this elution curve to explain the action of a gel filtration column. Explain the fact that phenol red is present in both colored fractions. In what fraction is the bovine serum albumin ... 

Figure B5.2.1 CPA hydrophobicity of bovine serum albumin. A quadratic model was fitted to the plot of net RFI versus protein concentration. The data point for the blank (buffer + probe) was included in the regression analysis for curve 1, but not for curve 2. Curve 2 gives a larger y-intercept and less steep slope. From Nakai et al. (1996) with permission from Kluwer Academic Publishers.

It has been observed that acidic drugs exhibit strong binding affinities for the serum albumins. Strong CD is induced in sulfaethidole when this compound binds to either crystalline or fraction V bovine serum albumin [68]. The data... 

---