Function of BSA concentration

Add distilled water so that the volume in the cuvettes is 1.6 ml, and finally make up the volume to 2 ml by adding 0.4 ml of Coomassie Blue. Mix slowly, then measure the OD at 595 nm. Plot the OD as a function of BSA concentration (standard plot). 

Fig. 9. Single- and triple-quantum filtered 87 Rb spectra as a function of BSA concentration. The triple-quantum creation time was set to rmax for each sample. The triplequantum filtered spectrum (10240 scans) is plotted above the corresponding singlequantum spectrum (64 scans). The downfield peak in the single-quantum spectrum is a Rb and KI reference. From Ref. 72, with permission.

Figure 14. Three-dimensional surface plot of the interfacial capacitance as a function of BSA concentration and applied interfacial potential. Water 0.01 mol/L LiCl nitrobenzene 0.01 mol/L TBATPB t = 25.0 °C. Interfacial potential U given vs. TBA + ion selective electrode. (Reproduced with permission from reference 32. Copyright 1990 Elsevier.)...

These results were extended by Tilton et a/.(n8) to adsorption of eosin-labeled BSA on polymer surfaces. They also found a component that surface diffuses, with coefficients ranging from 1.2 x 10 9 to 2.6 x 10 9cm2/s, depending on surface type. In this study, intersecting TIR laser beams rather than a focused stripe were used to define the spatial intensity variation. Surface diffusion was even noted for the most irreversibly adsorbed eosin-labeled BSA components this was evident on samples rinsed for long periods with unlabeled BSA after exposure to eosin-labeled BSA. The surface diffusion coefficient of the irreversibly bound BSA was found to be a strong function of adsorbed concentration.(n9)... 

Titration of a constant concentration of BSA with TNS yields a decrease in the fluorescence intensity of the Trp residues together with an increase in the fluorescence intensity of TNS (not shown). We do not observe an isoemissive point at either pH, thus indicating that TNS has more than one binding site on BSA. After correcting the fluorescence intensities at the emission peak of Trp residues for the dilution and then for the optical densities at the excitation (Xex = 280 nm) and emission wavelengths (335 or 325 nm), we can plot the fluorescence intensity as a function of TNS concentration at pH 3 and 7 (Figure 15.3). Results indicate that the fluorescence-intensity decrease is more important at pH 3 than at pH 7. This means that the interaction between TNS and BSA is more important at a low pH. 

Comparison of equilibrium adsorption (Figures 4 and 5) and minute protein adsorption/flocculation as a function of protein concentration, Cp, demonstrates strong but variable effects of pH and salinity.4 The equilibrium adsorption of proteins is as large as 1 mg/m2 (or 300 mg/g) at pH 3.5 (i.e. between pH(IEP) of silica and proteins) for bovine serum albumin (BSA) with 0.9 wt.% NaCl and gelatin without NaCl, or at pH(IEP) of protein for ovalbumin without NaCl. The lowest equilibrium adsorption (0.1-0.2 mg/m2) is typically observed at pH = 2, which is close to pH(IEPS o2) 2.2, and without NaCl (Figure 4). It should be... 

Figure 12. Potential of zero charge of the water-nitrobenzene inteface as a function of varying concentration of BSA in log (ppm). Supporting electrolytes 0.01 mol/L LiCl in water 0.01 mol/L TBATPB in nitrobenzene.

Figure 10. Desorption plot of BSA on amine-coated surface showing the relationship between the percent of desorbable protein as a function of applied concentration and flow rate (0.05 M Tris/HCl, pH 7.4, 0.02% NaN3, 25°C). Key of flow rates , 0.672 mLlmin , 0.277 mLlmin o, 0.150 mL/min and , 0.087 mLlmin.

Figure 4 shows the results of U of the complexes as a function of the concentration of BSA Cbsa - In the region of Cbsa < 60 pmoldm , the values were almost constant. In the region of Cbsa > 60 pmol dm they increased with increasing Cbsa and attained the constant value at Cbsa = 122pmoldm" at which a saturated complex is considered to be formed. 

The increase of D as a function of salt concentration c at constant polyelectrolyte concentration is already reported in one of the earhest studies on polyelectrolyte solutions by Doherty and Benedek on BSA [217]. The appearance of the slow diffusion process upon variation of c, at constant Cp was first detected by Schurr et al. on PLL solutions [218]. Drifford and Dalbiez [219] demonstrated that the slow and fast diffusion processes occur simultaneously. Moreover, the increase of D with decreasing salt at constant polyelectrolyte concentration has been observed for BSA [204,220], poly (L-lysine) [221-223], DNA [133]. heparin [190], NaPSS [210, 219], QPVP [9], hyalonurate [213], proteoglycane [133], chondroitin-6-sulfate [210], and crosslinked NaPAA [224] (Fig. 11). The onset of the transition regime II at X 1 has been found for poly(L-lysine) [218,221], hyalonurate [213], proteoglycan [133] and NaPSS [219]. 

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.]...

For each TNS concentration, measure the intensity variation A I, and then plot 1/Af as a function of 1/[TNS]. By extrapolating to 1/[TNS] = 0, we can calculate AImax. Is AImax the same for both pHs Explain. Determine the apparent value of the association constant Jassociation constants equal Explain. 

Figure 15.6 3D plots of Acridan assay emission as a function of time from glass slides without (Top) and with low power microwave exposure / pulses (Middle). Bottom - photographs showing the Acridan emission both before (a) and after a low power microwave pulse (b). Mw - Microwave pulse. The concentration of BSA-Biotin was 1.56 pM. Adopted from Ana/ Chem 78 8020-8027 (2006). 

The efficacy of Dy(PPP)2 and Dy(TTHA)3- as shift reagents for a variety of ions, including 23Na+, 39K+ and 87Rb+, has been examined,7 and the effect of temperature, osmolarity and shift reagent concentration on the chemical shift has been studied by Burnstein and Fossel.63 The chemical shift of 87Rb+ as a function of Dy(TTHA)3- concentration in the presence of 6.7 g% bovine serum albumin (BSA) is shown in Fig. 8. The BSA was included to mimic the extracellular plasma environment. 

Fig. 8. (A) The chemical shift of 10 mM RbCl in 6.7 g% BSA as a function of Dy(TTHA)3- concentration. (B) The 87Rb+ linewidths as a function of the Dy(TTHA)3-...

Protein and Lipid-Protein Systems. The high surface viscosity of BSA and the low surface viscosity of RNase had been observed by a torsion rotational method that used an extremely large torque (2, 6). In the present experiments, the protein is dispersed in the aqueous subphase to a final concentration of 10 /xg/ml. Both film pressure and surface viscosity are measured as a function of time (to 40 min). The film pressure of BSA was 21 dynes/cm at mixing and remained constant for 40 min. Also, surface viscosity reached a high value instantaneously (although the first measurement was made at 5 min) and remained constant for 40 min. In contrast, RNase built up pressure slowly, from 3 dynes/cm... 

SOS spectrum. SOS spectra of different components are shown in Fig. 1. This shows that the scattering intensity of BSA or M4MRASP itself was quite weak, either in the acidic medium or with SDS. However, when BSA was injected into M4MRASP in the presence of SDS, the scattering intensity was enhanced sharply (curve 5). The scattering intensity became stronger with an increase in the BSA concentration, and there was a functional relationship between the concentration of BSA and scattering intensity. 

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