Serum proteins mobilities

Wl. Waldmann-Meyer, H., and Schilling, K., Determination of free protein mobilities by paper electrophoresis with evaporation. II. Evaluation of temperature and concentration increases, influence of the carrier medium, and measurement of serum protein mobilities. Acta Chem. Scand. 13, 13-28 (1959). 

Nakamura, T., Fujiwara, N., Sato, E., Kawagoe, Y., Ueda, Y., Yamada, S., Koide, H. Effect of polymyxin B-immobilizcd fiber hemoperfusion on serum high mobility group box-1 protein levels and oxidative stress in patients with acute respiratory distress syndrome. ASAIO J 55... 

Figure 1. Systematic variation of molar ratio of ala to thr with mobility of electrophoretic components of serum proteins...

Figure 1 shows diagrammatically the arrangement of the proteins of the serum in accordance with their mobilities, as would be found in a classical electrophoretical pattern obtained by electrophoresis of normal serum at pH 8.6 in veronal buffer. The Bence-Jones and myeloma globulins are also placed in areas where they were found in respect to the serum proteins indicated (see Table V for other data on these proteins). In each system, in both the hepatic and extrahepatic proteins (26), the ala-thr ratios change in the same direction as the... 

Electrophoretic evaluation of the mucous substances of the gastric juice is complicated by the somewhat similar electrophoretic mobilities of serum proteins and their degradation products. Serum albumin has a mobility only slightly more negative than that of mucoprotein in M2 (Fig. 4). The first anodic degradation product of albumin has a mobility identical with that of component M3a (Fig. 4). The second anodic degradation product of serum is localized on the electrophoretic partition very close to component M3b (Fig. 5). Finally, the mobility of y-globulin is identical with that of component XI. 

Fig. 3 Countercurrent chromatographic separation of HDL-LDL and VLDL-serum protein fractions from human serum with an aqueous polymer phase system. Column 2.6mm I.D. PTFE single-layer coil (x2) with 60-mL capacity sample 4 mL of human serum solvent system 16% PEG 1000-12.5% dibasic potassium phosphate at pH 9.2 mobile phase lower phase flow rate 0.5 mL/min revolution speed 500 rpm. SF = solvent front, UP = starting point of the reversed elution mode with the upper phase.

One problem associated with conventional electrophoresis of serum proteins is its proclivity for point-of-application artifacts. These are bands that result from the fact that electrophoretic mobility (e.g., with AGE) is bidirectional from the point of application. Consequently the point of application remains part of the scanned area of interest. The fact that these must be immunotyped to distinguish real monoclonal proteins from artifacts is costly and time consuming. 

Schultze, H. E., Influence of bound sialic acid on electrophoretic mobility of human serum proteins. Arch. Biochem. Biophys. Suppl. 1, 290-294 (1962). 

An older man with severe emphysema is found to have decreased amounts and abnormal mobility of tti antitrypsin (AAT) protein in his serum when analyzed by serum protein electrophoresis. Liver biopsy discloses mild scarring (cirrhosis) and demonstrates microscopic inclusions due to an engorged endoplasmic reticulum (ER). The most likely explanation for these findings is... 

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