Plasma electrophoresis

Ruther E., Wiltfang, J. (2004b). Electrophoretic separation of amyloid P peptides in plasma. Electrophoresis 25, 3336-3343. 

RB Taylor, S Toasaksiri, RG Reid. A literature assessment of sample pretreatments and limits of detection for capillary electrophoresis of drugs in biological fluids and practical investigation with some antimalarials in plasma. Electrophoresis 19 2791-2797, 1998. 

Schappler, J., Guillarme, D., Prat, J., Veuthey, J.-L., and Rudaz, S. Enhanced method performances for conventional and chiral CE-ESI/MS analyses in plasma. Electrophoresis, 27, 1537, 2006. 

Albumin. Investigation iato the safety of bovine plasma for clinical use was undertaken ia the eady 1940s ia anticipation of wartime need (26). Using modem proteia chemistry methods, including electrophoresis and ultracentrifugation, it was shown that most of the human adverse reactions to blood substitutes were caused by the globulin fraction and that albumin was safe for parenteral use. Human albumin is now used extensively as a plasma expander ia many clinical settings. 

The number of different proteins in a membrane varies from less than a dozen in the sarcoplasmic reticulum to over 100 in the plasma membrane. Most membrane proteins can be separated from one another using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), a technique that has revolutionized their study. In the absence of SDS, few membrane proteins would remain soluble during electrophoresis. Proteins are the major functional molecules of membranes and consist of enzymes, pumps and channels, structural components, antigens (eg, for histocompatibility), and receptors for various molecules. Because every membrane possesses a different complement of proteins, there is no such thing as a typical membrane structure. The enzymatic properties of several different membranes are shown in Table 41-2. 

The fundamental role of blood in the maintenance of homeostasis and the ease with which blood can be obtained have meant that the study of its constituents has been of central importance in the development of biochemistry and clinical biochemistry. The basic properties of a number of plasma proteins, including the immunoglobulins (antibodies), are described in this chapter. Changes in the amounts of various plasma proteins and immunoglobulins occur in many diseases and can be monitored by electrophoresis or other suitable procedures. As indicated in an earlier chapter, alterations of the activities of certain enzymes found in plasma are of diagnostic use in a number of pathologic conditions. 

Microwave plasma detection has been reviewed [351], also in relation to GC [352,353], Coupling of chromatography (GC, SFC, HPLC) and capillary electrophoresis (CE) with ICP-MS and MIP-MS detectors has also been reviewed [181,334,335]. Various specific GC-ICP-MS reviews have appeared [334,337,345,346,354,355]. 

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. 

Weekes J et al. Bovine dilated cardiomyopathy proteomic analysis of an animal model of human dilated cardiomyopathy Electrophoresis 1999 20 898-906. Doherty NS et al. Analysis of changes in acute phase plasma proteins in an acute inflammatory response and in rheumatoid arthritis using two-dimensional gel electrophoresis. Electrophoresis 1998 19 355-363. 

In the analysis of clinical, biological and environmental samples it is often important to have information on the speciation of the analyte, e.g. metal atoms. Thus an initial sample solution may be subjected to a separation stage using chromatography or electrophoresis. Measurements may, of course, be made on fractions from a fraction collector, but with plasma sources, interfacing in order to provide a continuous monitoring of the column effluent can be possible. This relies upon the ability of the high-temperature plasma to break down the matrix and produce free ions. 

A number of workers have utilised electrophoresis to establish the formation of a complex between neomycin and the proteins in blood-serum and plasma- - -, 105,106,107,108,109,110,111. However, the nature of the complex is still unknown. Geitman has extensively studied the phenomena of protein-binding of antibiotics- -- -- - > 112. ... 

The hollow fiber was dipped into dihexyl ether for 5 sec and excess adhering solvent was washed away by ultrasonification in a water bath. Then, 25 fiL of lOmM hydrochloric acid (aqueous, acceptor phase) was injected into the lumen of the hollow fiber with a microsyringe. This activated fiber was placed in the vial containing the donor solution and the vial vibrated at 1500 rpm for 45 min. The entire acceptor solution was flushed into a 200-fJ.L micro insert and subjected to capillary electrophoresis or HPLC detection. For 2 mL extractions, 250 //I. of plasma sample treated with... 

Finally, work that may facilitate understanding the role of oq-acid glycoprotein variants in inter-individual variations in plasma protein binding, pharmacokinetic behavior, and drug action has been described. A capillary zone electrophoresis method that allows for the determination of 11 intact forms (i.e., isoforms, glycoforms) of oq-acid glycoprotein has been described [84],... 

Electrophoresis of the urine in these cases with more massive proteinuria shows a protein pattern resembling plasma (K13). 

Smithies vertical starch gel electrophoresis (S7) separates the plasma proteins more distinctly than any other method. If the Hp concentration is normal, the Hp type can generally be recognized directly after the staining for proteins, but sensitive and more specific staining for heme groups, e.g., benzidine, o-dianisidine (04), and malachite green (N5) are preferable. This technique consumes more hydrolyzed starch than the simpler original horizontal electrophoresis technique (S5). 

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