Serum electrophoresis

Latner AL, Marshall T, Gambie M. A simplified technique of high-resolution two-dimensional electrophoresis serum immunoglobulins. Clin ChimActa 1980 103 51-59. 

Figure 4-21. Serum electrophoresis. Serum electrophoresis is the separation of serum proteins by simple zonal electrophoresis. It is usually carried out under slightly alkaline conditions where most of the proteins or classes of protein are negatively charged and thus migrate towards the anode.

A. Familial lipoprotein lipase deficiency (Type I lipoprotein pattern on electrophoresis). Serum triglycerides become elevated with particular elevation of chylomicrons. Tliere are xanthomas, rather than atherosclerosis. Pancreatitis may result from the action of pancreatic lipase on these elevated chylomicrons, with resultant excess triglyceride breakdown in the pancreas, pancreatic injury, and release of more pancreatic lipase. (Note that the body contains different kinds of lipases. There is a pancreatic lipase, which is a digestive enzyme a lipoprotein lipase, which is an extracellular enzyme that breaks down plasma triglycerides, thereby enabling fatty acids to enter cells and an intracellular lipase that breaks down stored triglycerides). 

Nonptotein artifact of CK-BB associated with albumin fraction of protein electrophoresis Serum protein electrophoresis, CK fractionation by ion-exchange chromatography... 

Cellulose acetate, polyacrylamide gel electrophoresis, serum proteins. Introduction... 

A. W. K. Tiselius (Uppsala) electrophoresis and adsorption analysis, especially for discoveries concerning the complex nature of the serum proteins. 

Douglas et al. [98] have measured protein (serum albumin, ovalbumin, and hemoglobin) mobilities over a range of pH values using a free-flow electrophoresis apparatus and a particle electrophoresis apparatus. They found good agreement between the two measurements however, they also found some differences between their measurements and those reported in the older literature. They attributed the differences to the use of moving-boundary electrophoresis methods in the early experimental work and to differences in... 

Figure 7-11. Normal and pathologic patterns of lactate dehydrogenase (LDH) isozymes in human serum. LDH isozymes of serum were separated by electrophoresis and visualized using the coupled reaction scheme shown on the left. (NBT, nitroblue tetrazolium PMS, phenazine methylsulfate). At right is shown the stained electropherogram. Pattern A is serum from a patient with a myocardial infarct B is normal serum and C is serum from a patient with liver disease. Arabic numerals denote specific LDH isozymes.

Figure 50-2. Technique of cellulose acetate zone electrophoresis. A A small amount of serum or other fluid is applied to a cellulose acetate strip. B Electrophoresis of sample in electrolyte buffer is performed.

Alkaline phosphatase assays based on 3-glycerophosphate now appears to be obsolete, and methods buffered by either glycine or barbital are also obsolete as these buffers inhibit ALP or are poor buffers. Serum alkaline phosphatase is known to be composed of several isoenzymes which presumably arise from bone, liver, intestine, and placenta. The placental alkaline phosphatase is known to be much more resistant to heat denaturation than the other isoenzymes, and this resistance provides a simple test for it (5). The other enzymes can be separated through the differential inhibition by phenylalanine, by electrophoresis and by specific antibodies. However, the clinical usefulness of the results obtained is in doubt (23). 

Shaw, C.F. Ill, Schaeffer, N.A., Elder, R.C., Eidsness, M.K., Trooster, J.M. and Calls, G.H.M. (1984) Bovine serum albumin-gold thiomalate complex gold-197 Moessbauer, EXAFS and XANES, electrophoresis, sulfur-35 radiotracer, and fluorescent probe competition studies. Journal of the American Chemical Society, 106, 3511-3521. 

Oda RP, Clark R, Katzman JA, Landers JP (1997) Capillary electrophoresis as a clinical tool for the analysis of protein in serum and other body fluids. Electrophoresis 18 1715-1723. 

Torres, A. R., Krueger, G. G., and Peterson, E. A., Purification of Gc-2 globulin from human serum by displacement chromatography a model for the isolation of marker proteins identified by two dimensional electrophoresis, Anal. Biochem., 144, 469, 1985. 

Kilar, E and Hjerten,S., Fast and high resolution analysis of human serum transferrin by high performance isoelectric focusing in capillaries, Electrophoresis, 10, 23, 1989. 

Kilar, F. and Fanali, S., Separation of tryptophan-derivative enantiomers with iron-free human serum transferrin by capillary zone electrophoresis, Electrophoresis, 16, 1510, 1995. 

Thormartn, W., Meier, R, Marcolli, C., and Binder, F., Analysis of barbiturates in human serum and urine by high-performance capillary electrophoresis-micellar electrokinetic capillary chromatography with on-column multiwavelength detection, /. Chromatogr., 545, 445, 1991. 

Heegard, N. H. H. and Robey, R A., Use of capillary zone electrophoresis to evaluate the binding of anionic carbohydrates to synthetic peptides derived from human serum amyloid P component, Anal. Chem., 64, 2479, 1992. 

AC ADME ANS AUC BA/BE BBB BBM BBLM BCS BLM BSA CE CHO CMC CPC CPZ CTAB CV DA DOPC DPPC DPPH aminocoumarin absorption, distribution, metabolism, excretion anilinonaphthalenesulfonic acid area under the curve bioavailability-bioequivalence blood-brain barrier brush-border membrane brush-border lipid membrane biopharmaceutics classification system black lipid membrane bovine serum albumin capillary electrophoresis caroboxaldehyde critical micelle concentration centrifugal partition chromatography chlorpromazine cetyltrimethylammonium bromide cyclic votammetry dodecylcarboxylic acid dioleylphosphatidylcholine dipalmitoylphosphatidylcholine diphenylpicrylhydrazyl... 

Apart from its natural occurrence, Co may find its way into other proteins either adventitiously or deliberately. A study was undertaken where the blood, serum, and plasma of workers occupationally exposed to Co were analyzed for the element.1189 When separated by gel electrophoresis under denaturing conditions, the Co fractions in all blood, serum, and plasma samples showed a similar protein pattern. A variety of proteins of differing size were found to bind Co in fractions collected at pFl 5, whereas only hemoglobin was found in the pH 7 fractions. The conclusions were that in vivo Co is bound to plasma proteins, perhaps albumin and hemoglobin. 

Valproic acid has been determined in human serum using capillary electrophoresis and indirect laser induced fluorescence detection [26], The extract is injected at 75 mbar for 0.05 min onto a capillary column (74.4 cm x 50 pm i.d., effective length 56.2 cm). The optimized buffer 2.5 mM borate/phosphate of pH 8.4 with 6 pL fluorescein to generate the background signal. Separation was carried out at 30 kV and indirect fluorescence detection was achieved at 488/529 nm. A linear calibration was found in the range 4.5 144 pg/mL (0 = 0.9947) and detection and quantitation limits were 0.9 and 3.0 pg/mL. Polonski et al. [27] described a capillary isotache-phoresis method for sodium valproate in blood. The sample was injected into a column of an EKI 02 instrument for separation. The instrument incorporated a conductimetric detector. The mobile phase was 0.01 M histidine containing 0.1% methylhydroxycellulose at pH 5.5. The detection limit was 2 pg/mL. 

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