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Protein effluent profile

Experimental interest lies in the value of q that depends on the applied concentration, that is, where q =/(c), which thus describes the isotherm-of the adsorbate. Application of protein solution to the column produced an effluent profile of the type shown in Figure 5. The amount of protein adsorbed may be calculated by integrating the area between the void volume and the actual effluent profile (lateral diffusion, DM, does not modify the integrated area). A series of runs using different cG values thus establishes a dynamic isotherm. [Pg.253]

Aside from the relative position of the profile, the shape of the effluent profile contains information concerning the kinetics of the adsorption process. All concentrations of protein from zero to cQ are brought into contact with the column surface as the protein solution flows through the column, as a function of the position of the profile, and therefore as a function of time. Working with small molecules, previous researchers have shown that compounds exhibiting Langmuir isotherms produce sharp fronts, and diffuse tails, if pure solvent is used to desorb the column (21,22). However, Equation 7 shows that both diffusional and adsorption effects can alter the shape of the effluent profile. The former effect includes both normal molecular diffusion, and also diffusion due to flow properties in the column (eddy diffusion), which broadens (decreases the slope) the affluent profiles. To examine the adsorption processes, apart from the diffusional effects, the following technique can be applied. [Pg.254]

Alternatively, the saturated substrate may not be inert to new solution-borne protein molecules, but may exchange with such molecules (23). The result of such a process, which does indeed occur as will be shown later, does not appear to alter adsorption effluent profiles. [Pg.256]

Rockabrand, D. Austin, T. Kaiser, R. Blum, P Bacterial growth state distinguished by single-cell protein profiling Does chlorination kill coliforms in municipal effluent Appl. Environ. Microbiol. 1999,65,4181-4188. [Pg.17]

Fig. 4.5. (A) Typical chromatogram of a standard mixture of 0.02 Mmole each of the protein-constituent amino acids resolved in a single 24-h run by the gradient shown in B. (B) The pH gradient profile obtained via mixing of the three buffers (pH 2.58, 3.80 and 12.00) from their reservoirs. The pH before zero time is determined with buffer of pH 2.72 in the buffer delivery lines from the mixer to the top of the columns. The effluent pH obtained from the mixer at zero time is 2.63. Fig. 4.5. (A) Typical chromatogram of a standard mixture of 0.02 Mmole each of the protein-constituent amino acids resolved in a single 24-h run by the gradient shown in B. (B) The pH gradient profile obtained via mixing of the three buffers (pH 2.58, 3.80 and 12.00) from their reservoirs. The pH before zero time is determined with buffer of pH 2.72 in the buffer delivery lines from the mixer to the top of the columns. The effluent pH obtained from the mixer at zero time is 2.63.
FIGURE 37 The upper panel (a) shows the time concentration curves for the loading of a HPLC-BMC column (Cibacron Blue F3GA Fractosil 1000 with HEWL) to an effluent concentrations of 2, 20, and 99% of the influent concentration, respectively, followed by washing, (b) The lower panel shows the concentration profiles in the solid phase corresponding to the numbered times the upper for this protein-sorbent combination. Data adapted from Ref. 8. [Pg.203]

Figure 9. Exchange of BSA by fibronectin on amine-coated surface. Profiles illustrate the molar concentrations of each protein in the column effluent. The dashed line indicates the void volume, or the point at which the BSA solution is just displaced from the column by the fibronectin solution (0.05 M Tris/HCl, 0.02% NaN3, pH 7.4, 0.15 mL/min, 37°C). Key , fibronectin T, BSA monomer and A, BSA dimer. Figure 9. Exchange of BSA by fibronectin on amine-coated surface. Profiles illustrate the molar concentrations of each protein in the column effluent. The dashed line indicates the void volume, or the point at which the BSA solution is just displaced from the column by the fibronectin solution (0.05 M Tris/HCl, 0.02% NaN3, pH 7.4, 0.15 mL/min, 37°C). Key , fibronectin T, BSA monomer and A, BSA dimer.
Since the major part of incorporated radioactivity was located in the 105,000 X g supernatant fraction from drug-treated cells, this fraction was separated into subtractions on a column of Sephadex G-200. The 105,000 X g supernatant fluid, which contains proteins, sRNA and soluble enzymes, as well as other cellular components, separates on a column of Sephadex G-200 into 3 peaks (Kadaya et al., 1964) when measured by absorbancy at 260 mp. (Fig. 3). Fig. 3 shows that the radioactivity of the control separated into two peaks, with the major portion of radioactivity eluted between the first and second absorbancy peak. A small portion of radioactivity was eluted in the third absorbancy peak. In contrast to the control, radioactivity of 105,000 X g supernatant fraction of drug-treated cells was eluted as a single peak, with the third absorbancy peak (Fig. 4). Radioactivity of this peak was equal to that of the control. Paper chromatography of the third peak fractions revealed the presence of nucleotides and small peptides, with edeine as the major radioactive component. When the protein content of the effluents from the column was determined by the Lowry method (Lowry 1951) all samples separated into 3 peaks as shown in Fig. 3. A comparison of protein and radioactivity profiles reveals that the inhibitors of protein synthesis affected the incorporation of tyrosine or methionine into protein fractions eluted between the first and second absorbancy peaks, leaving unaffected incorporation into the edeine containing third peak. [Pg.348]


See other pages where Protein effluent profile is mentioned: [Pg.252]    [Pg.328]    [Pg.30]    [Pg.204]    [Pg.211]    [Pg.115]    [Pg.223]    [Pg.237]    [Pg.377]    [Pg.362]   
See also in sourсe #XX -- [ Pg.256 ]




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