Bovine serum albumin kinetics

Ovalbumin and bovine serum albumin Kinetic and equilibrium studies of the acid and urea denatura-tions were followed by AAjsto, by a, by ri, and by s Glazer and McKenzie (1962a)... 

The flux of 3H-labeled PNU-78,517 across MDCK cell monolayers shows the characteristic disparity between the kinetics of disappearance from the donor solution and appearance in the receiver sink (Fig. 32). Drug uptake is rapid and exponential with time and approaches a quasi-equilibrium state in contrast, the concomitant efflux of drug into the receiver is slow and linear. While maintaining a 3% bovine serum albumin (BSA) concentration in the donor and varying the BSA concentration between 0.5 and 5% in the receiver, the results show that the... 

Figure 32 Disappearance and appearance kinetics of transcellular flux of the lipophilic antioxidant PNU-78,517 (pKa 6.5) across MDCK cell monolayers in Transwell systems at 37°C. Donor solutions contained 3% bovine serum albumin (BSA), and receiver solutions contained 0.5-5% BSA at pH 7.4. [Redrawn from Raub et al. (1993) with permission from the publisher.]... 

In this connection, the use of insoluble agents as photosensitizers seems promising. This approach, in particular, has been realized in respect to the suspension of crystal fullerene C60 (Kasermann and Kempf, 1997, 1998). Its marked advantage is that there are no byproducts of the destruction of fullerene and the compound can be easily removed from the solution by centrifugation. The high efficiency of C60 in viral inactivation has been demonstrated for specific enveloped viruses such as Semliki forest vims (SFV) and vesicular stomatitis vims (VSV) (Kasermann and Kempf, 1997, 1998). The inactivation was achieved in a model system where the vims was suspended in a saline buffer solution. The addition of 2% bovine serum albumin did not affect the kinetics of the photoinactivation of the vims. 

Any detectable effect on the reaction or behavior of a particular system by the interior wall of the container or reaction vessel. Because proteins can form high-affinity complexes with glass and plastic surfaces, one must exercise caution in the choice of reaction kinetic conditions. Wall effects can be discerned if one determines catalytic activity under different conditions that minimize or maximize contact of the solution with the container. In principle, an enzyme-catalyzed reaction should proceed at the same rate if placed in a capillary or a culture tube however, contact with the wall is maximized in a capillary, and wall effects should be more prominent. Some investigators add bovine serum albumin to prevent adsorption of their enzyme onto the container s walls. 

Urea in kidney dialysate can be determined by immobilizing urease (via silylation or with glutaraldehyde as binder) on commercially available acid-base cellulose pads the process has to be modified slightly in order not to alter the dye contained in the pads [57]. The stopped-flow technique assures the required sensitivity for the enzymatic reaction, which takes 30-60 s. Synchronization of the peristaltic pumps PI and P2 in the valveless impulse-response flow injection manifold depicted in Fig. 5.19.B by means of a timer enables kinetic measurements [62]. Following a comprehensive study of the effect of hydrodynamic and (bio)chemical variables, the sensor was optimized for monitoring urea in real biological samples. A similar system was used for the determination of penicillin by penicillinase-catalysed hydrolysis. The enzyme was immobilized on acid-base cellulose strips via bovine serum albumin similarly as in enzyme electrodes [63], even though the above-described procedure would have been equally effective. 

Anand, K., Damodaran, S. (1995). Kinetics of adsorption of lysozyme and bovine serum albumin at the air/water interface from a binary mixture. Journal of Colloid and Interface Science, 176, 63-73. 

Krisdhasima, V., Vinaraphong, R, and McGuire, J. 1993. Adsorption kinetics and elutability of a-lactalbumin, p-casein, p-lactoglobulin and bovine serum albumin at hydrophobic and hydrophilic interfaces. J. Colloid Interface Sci. 161 325-334. 

Solutions of acid phosphatase are particularly sensitive to surface inactivation. Figure 3 (88) shows the inactivation rate of the enzyme in the presence and absence of surface-active detergents. The inactivation process is temperature sensitive and the protection by detergent is total. Most of the enzyme inactivation proceeds with first-order kinetics. A variety of agents—gelatin, bovine serum albumin, egg albumin, and Tween-80—protect the enzyme against inactivation. 

T.W.C. Lo, M.E. Westwood, A.C. McLellan, T. Selwood, and PJ. Thomalley, Binding and modification of proteins by methylglyoxal under physiological conditions a kinetic and mechanistic study with A,K-acelyIargi ni nc, -acetylcysteine, and A -acetyllysine, and bovine serum albumin. J. Biol. Chem., 1994, 269, 32299-32305. 

Capper (II) Transfer from Serum Albumin (13). The kinetics of transfer of Cu(II) from its complexes with human serum albumin, bovine serum albumin, gly-gly-his, gly-gly-his-gly, and asp ala his Tys to trien all exhibit parallel behavior. The histidine-containing peptides model the first Cu(II) binding site in the serum albumins, where Cu(II) is coordinated to the amine terminal, to two deprotonated peptide nitrogens,... 

UV photolysis of CpMn(CO)3 in toluene leads to loss of CO and formation of CpMn(CO)2( ] -toluene). Kinetic studies suggest that the binding energy of the toluene is ca. 60kJmor. The binding of H2 to CpMn(CO)2 has been studied in supercritical CO2 solvent. It has been proposed that pyrylium and pyridinium salts such as (35) can be used to label proteins and thereby aid in the detection and characterization of receptor sites. Cymantrene bound to lysine residues of bovine serum albumin (BSA) has been used as a redox label. Electrochemical reduction of the label established an impressive BSA detection limit of 2 x 10 M. 

Besides the conventional factors causing peak broadening in LC. another source for lower efficiency in LC with chiral stationary phases may be the existence of at least two different adsorption sites (the stereoselective and non-stereoselective ones) that may considerably differ in their adsorption kinetics (heterogeneous mass transfer kinetics) and thus cause peak broadening and tailing. These factors have been investigated and modelled by Fomstedt et al.. e.g. for protein type CSPs [75,91-9.3] and their contribution was determined for different analytes and different type of CSPs (bovine serum albumin, cellobiohydrolase 1, tris(4-methylbenzoyl) cellulose) [94j. In a recent study, these authors reported on the adsorption isotherms as well as selective and nonselective contributions of propranolol enantiomers on a cellobiohydrolase 1 CSP in dependence of the mobile phase pH [95[. 

Fig. 2. Kinetics of displacement of segments from a bovine serum albumin mono-layer at 16 mN m I x is the change of distance between barriers and is proportional to the change of the area xe is the value of x at which equilibrium is established. From MacRitchie (1963).

Giimusderelioglu M, Kesgin D (2005) Release kinetics of bovine serum albumin from pH-sensitive poly(vinyl ether) based hydrogels. Int J Pharm 288 273-279... 

Fig. 9.12 Variations in HGL (full symbols) and RGL (open symbols) activity during incubation with orlistat in the absence (circles) or presence (triangles) of 4 mM NaTDC. Lipases (26 pM) were incubated at 37°C, in a final volume of 150 pL of 50 mM acetate buffer (pH 6.0), 150 mM NaCl with orlistat (2.6 mM). Residual lipase activity was measured at pH 6.0, 37°C by tributyrin (0.2 mL) hydrolysis using 10 mL of 150 mM NaCl, 2 mM NaTDC, 1.5 pM bovine serum albumin. Each kinetics represents one experiment. Adapted from [51].

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