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Buffer protein

Membrane-retained components are collectively called concentrate or retentate. Materials permeating the membrane are called filtrate, ultrafiltrate, or permeate. It is the objective of ultrafiltration to recover or concentrate particular species in the retentate (eg, latex concentration, pigment recovery, protein recovery from cheese and casein wheys, and concentration of proteins for biopharmaceuticals) or to produce a purified permeate (eg, sewage treatment, production of sterile water or antibiotics, etc). Diafiltration is a specific ultrafiltration process in which the retentate is further purified or the permeable sohds are extracted further by the addition of water or, in the case of proteins, buffer to the retentate. [Pg.293]

For precipitated protein, buffered solutions containing chaotropic reagents such as 0.1% SDS, 8 M urea, or 6 M guanidine or proteolytic enzymes such as pepsin may be used. However, an extended washing with buffer is required to remove SDS and guanidine. Unexpected elution behavior can occur if these reagents are not removed completely. [Pg.135]

Extracellular bicarbonate and intracellular protein buffering systems... [Pg.420]

Young. But these are 10 free ions. There is protein buffering and so even though there are a huge number of ions there, only 10 are free. [Pg.183]

Prepare competitor protein buffer detergent solution 4 mg/mL normal goat globulin or other competitor protein, (such as fetal calf serum, bovine serum albumin, bovine plasma, and so forth), and 0.1% saponin (Sigma, St. Louis, MO) in phosphate-buffered saline (NGG-sap-PBS). [Pg.123]

Preparing Non-covalent Complexes in Protein Buffer Protein Concentration, Ligand Concentration, Incubation Time... [Pg.75]

C) mixture H2. Nearly all the ions are from the protein, buffer and solvent background except for the ions at m/z 145.8 and mjz 155.7. These two ions are protonated molecular ions for compounds with MWs of 145 Da and 155 Da that bind to MMP-1. Reprinted from reference [1] with permission from Elsevier Science. [Pg.106]

Figure 16.8 The excess heat capacity, C xcess = Cp (protein + buffer) - C/,(buffer), as a function of temperature, obtained from a differential scanning calorimeter. The shaded area is intergrated to yield the enthalpy of the transition. AtransCp is the difference in the baseline heat capacity at Tm. Figure 16.8 The excess heat capacity, C xcess = Cp (protein + buffer) - C/,(buffer), as a function of temperature, obtained from a differential scanning calorimeter. The shaded area is intergrated to yield the enthalpy of the transition. AtransCp is the difference in the baseline heat capacity at Tm.
An adverse external influx of acids could be removed by the protein buffer soaking up the H+ ions to form a positive ion, hence restoring the original pH. [Pg.144]

Haemoglobin (a compound of iron and proteins) buffers the blood system using the proteins present. This is essential for controlling the pH of the blood, which is necessary due to the uptake of acidic C02 gas formed when cells use carbohydrates, glucose, to give energy. [Pg.144]

The simulation results presented show clearly the dependence of the ISFET response on the concentration of protein immobilized in a membrane on top of the device. Since the number and type of proton dissociating groups determine the protein buffer capacity (dc rM/ dp ), and since the ISFET response directly reflects the change in pH as a function of time, in principle the shape of an ISFET response also contains information on the type of protein that is immobilized. [Pg.383]

The slope of the measured titration curve is inversely proportional to the buffer capacity of the protein, which contains specific information on the type of protein. After modification of the coulometric sensor-actuator device with a porous gold actuator electrode, the device is shown to be suitable for the determination of protein buffer capacity in solution [17]. A schematic representation of the device is shown in Fig. 12. The buffer capacity can be measured by sending a small alternating current through the porous actuator electrode, resulting in the alternating generation of protons and hydroxyl ions. This will result in a small pH perturbation in the free space of the porous electrode, which is detected by... [Pg.387]

J. R. Cann, Biochemistry, 5 1108-1112 (1966). Multiple Electrophoretic Zones Arising from Protein-Buffer Interaction. [Pg.232]

Load protein solution, (allow to adsorb, 1-5 min.) Total Adsorbed bulk protein, buffer... [Pg.477]

Flow 2ml buffer once through cell ( 10sec) Flush Tightly adsorbed protein, buffer... [Pg.477]

Intracellular fluids (also called the cytosol) are quite different compositionally from plasma and interstitial fluids (Table 4, Figures 4 and 5). The internal pH of many cells is maintained near 6.9-7.0. via various membrane transport mechanisms such as Na" /H and CP/HCO exchangers, and various phosphate and protein buffers. In contrast to the plasma, the intracellular fluids have substantially lower concentrations of sodium, calcium, chloride, and bicarbonate and higher to substantially higher concentrations of potassium, magnesium,... [Pg.4827]

Wu N, Sweedler JV, Lin M. Enhanced separation and deletion of sermn bilirubm species by capillary electrophoresis using a mixed anionic surfactant-protein buffer system with laser-induced fluorescence detection. J Chromatogr B Biomed Appl 1994 654 185-91. [Pg.1208]

Plasma Protein Buffer System and Plasma Base Excess The buffer value (p) of the nonbicarbonate buffers of plasma is about 7.7 mmol/L at pH 7.40 and a normal plasma protein concentration of 72 g/L. Proteins, especially albumin, account for the greatest portion (95%) of the nonbicarbonate buffer value of the plasma. The most important buffer groups of proteins in the physiological pH range are the imidazole groups of histidines (pimolecule contains 16 histidines. [Pg.1760]

Excess carbonic acid present in blood is to a great extent buffered by the hemoglobin and protein buffer systems (see Figure 46-9). The buffering of CO2 causes a slight rise in cHCOT Thus in the immediate posthypercapnic state,... [Pg.1774]

K23. Klotz, I. M., and Urquhart, J. M., The binding of organic ions by proteins buffer effect. J. Phya. Colloid Chem. 63, 100-114 (1949). [Pg.292]

The three most important buffers in the body are the bicarbonate buffer, the phosphate buffer, and the protein buffer. Each is adapted to solve specific physiological problems in the body. [Pg.89]


See other pages where Buffer protein is mentioned: [Pg.421]    [Pg.359]    [Pg.209]    [Pg.60]    [Pg.61]    [Pg.63]    [Pg.53]    [Pg.53]    [Pg.211]    [Pg.7]    [Pg.152]    [Pg.34]    [Pg.50]    [Pg.596]    [Pg.144]    [Pg.145]    [Pg.126]    [Pg.152]    [Pg.645]    [Pg.10]    [Pg.441]    [Pg.91]   
See also in sourсe #XX -- [ Pg.60 ]

See also in sourсe #XX -- [ Pg.60 ]




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