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Serum proteins relative mobilities

Fig. 3 SDS-PAGE Photograph Separation (Lane Mr and A) and activity staining (Lane B and C) of the crude filtrate of Funalia trogii. Lane Mr standard molecular weight markers ([3-galactosi-dase, 118.0 kDa bovine serum albumin, 79.0 kDa ovalbumin, 47.0 kDa carbonic anhydrase, 33.0 kDa P-lactoglobulin, 25.0 kDa and lysozyme, 19.5 kDa). Relative mobilities of the standard markers vs. common logarithms of their molecular masses were plotted.With the linear regression output, the molecular masses of the proteins in the crude filtrate were estimated (taken from [18])... Fig. 3 SDS-PAGE Photograph Separation (Lane Mr and A) and activity staining (Lane B and C) of the crude filtrate of Funalia trogii. Lane Mr standard molecular weight markers ([3-galactosi-dase, 118.0 kDa bovine serum albumin, 79.0 kDa ovalbumin, 47.0 kDa carbonic anhydrase, 33.0 kDa P-lactoglobulin, 25.0 kDa and lysozyme, 19.5 kDa). Relative mobilities of the standard markers vs. common logarithms of their molecular masses were plotted.With the linear regression output, the molecular masses of the proteins in the crude filtrate were estimated (taken from [18])...
Fig. 2.1. Semilogarithmic plot of molecular weight (Mr) of marker proteins vs relative mobility (Rf) of marker proteins in gels of different acrylamide concentrations %T. Proteins 1 aprotinin (6.5 kD) 2 lysozyme (14.5 kD) 3 soybean trypsin inhibitor (21.5 kD) 4 carbonic acid anhydrase (31 kD) 5 hen ovalbumin (45 kD) 6 bovine serum albumin (66 kD) 7 phosphorylase b (97.4 kD) 8 8-galactosidase (116 kD) 9 myosin (205 kD)... Fig. 2.1. Semilogarithmic plot of molecular weight (Mr) of marker proteins vs relative mobility (Rf) of marker proteins in gels of different acrylamide concentrations %T. Proteins 1 aprotinin (6.5 kD) 2 lysozyme (14.5 kD) 3 soybean trypsin inhibitor (21.5 kD) 4 carbonic acid anhydrase (31 kD) 5 hen ovalbumin (45 kD) 6 bovine serum albumin (66 kD) 7 phosphorylase b (97.4 kD) 8 8-galactosidase (116 kD) 9 myosin (205 kD)...
Fig. 11. Electrophoretic distribution in agar of gastric mucosal extract protein (A) protease activity at pH 2.2 (B) carboxylic esterase activity (C) and immuno-electrophoretic pattern (D). The relative mobility is shown at the bottom (UR) with 0 representing the location of the uncharged dextran, levan and 1 the migration of human serum albumin. The zones of mobility (Z), arbitrarily defined on the basis of protein distribution, are indicated at the top. Each antigen and enzyme is designated by the zone in which it is found. The antigens are alsc designated by a letter. From Kushner et al. (K32). Fig. 11. Electrophoretic distribution in agar of gastric mucosal extract protein (A) protease activity at pH 2.2 (B) carboxylic esterase activity (C) and immuno-electrophoretic pattern (D). The relative mobility is shown at the bottom (UR) with 0 representing the location of the uncharged dextran, levan and 1 the migration of human serum albumin. The zones of mobility (Z), arbitrarily defined on the basis of protein distribution, are indicated at the top. Each antigen and enzyme is designated by the zone in which it is found. The antigens are alsc designated by a letter. From Kushner et al. (K32).
Based upon such data, direct analysis of some fractions is possible when the components can be identified by their mobility alone. However, such an application is very limited in practice, as many subfractions have almost equal mobilities. In order to measure relative mobilities, it is practical to use pure serum albumin as reference. If the mobility of the latter is aib and the mobility of the unknown protein Ux, the quotient x/Waib is independent of the carrier medium if the migration velocity does not change during the run. In Table 3, relative mobilities... [Pg.237]

Likhtenshtein and colleagues (Belonogova et al., 1978, 1979 Likhten-shtein, 1976) carried out a series of measurements on the hydration dependence of the mobility of spin labels covalently bound to several proteins. The results were correlated with Mossbauer spectroscopic data obtained in parallel experiments. Spin-labeled human serum albumin and a-chymotrypsin showed a critical hydration level for onset of motion at relative humidity 0.8, equivalent to 0.2 h. The temperature dependence of the spin label spectrum showed a critical temperature of 230 K, below which motion was frozen. Serum albumin labeled at surface sites... [Pg.76]

Boyer and Hsu [1] studied the equilibrium adsorption of alcohol dehydrogenase onto Cibacron Blue F-3GA affixed to Sepharose CL-6B in a potassium phosphate, pH 7.0 mobile phase at 4°C and found that depending on the concentration of the immobilized dye, Ka fell in the range of 1.0 - 2.6T0- M. The relative effect of ligand concentration on Ka for various proteins based on the results of Boyer and Hsu are shown in Figure 4. Arnold and Blanch [7] have found that the Ka values fall within the range 1.1 - 1.3 10- M for bovine serum albumin adsorbing to Cibacron Blue Sepharose CL-4B. They also reported the variation of Ka for... [Pg.838]

Knowledge of the distance of electroosmotic flow is also important for the estimation of the mobilities of different ions relative to each other, as is often useful in work with filter paper. Without consideration of the water flow, calculated isoelectric points are erroneously high. In protein work this is particularly important for basic materials. The lower water flow in acid solution accounts for the small deviation of the isoelectric point of serum albumin as calculated by certain workers without measurement of the water flow (49,64). This result is expected on theoretical grounds and does not represent evidence against the general importance of electroosmotic water flow (41). Table I lists the results of measurements... [Pg.165]


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