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Serum proteins electrophoresis

Nonptotein artifact of CK-BB associated with albumin fraction of protein electrophoresis Serum protein electrophoresis, CK fractionation by ion-exchange chromatography... [Pg.81]

Cellulose acetate, polyacrylamide gel electrophoresis, serum proteins. Introduction... [Pg.436]

A. W. K. Tiselius (Uppsala) electrophoresis and adsorption analysis, especially for discoveries concerning the complex nature of the serum proteins. [Pg.1297]

Electrophoresis has also been employed to separate neomycin from analytically-interfering substances such as proteins. Hence Brammer and Hemsonl82 have determined the neomycin content of blood serum. Neomycin was separated from the serum proteins by electrophoresis on cellulose acetate and assayed colorimetrically following elution from the support. [Pg.440]

Fig. 1. Schematic presentation of the protein pattern of the common Hp types in pure form after starch-gel electrophoresis. The protein pattern of a normal serum belonging to Hp type 1-1 is given at the bottom. The cathodic part is excluded. Fig. 1. Schematic presentation of the protein pattern of the common Hp types in pure form after starch-gel electrophoresis. The protein pattern of a normal serum belonging to Hp type 1-1 is given at the bottom. The cathodic part is excluded.
Smithies, O., Zone electrophoresis in starch gels group variations in the serum proteins of normal human adults. Biochem. J. 61, 629 (1955). [Pg.186]

Figure 3.25 Starch gel electrophoresis of human serum proteins. Samples 1 and 2 are normal while samples 3, 4 and 5 show an extra band adjacent to the normal albumin which is due to the presence of bis-albumin. Sample 7 contains a myeloma protein that has remained near the origin. (Photograph by permission of Dr D. Brocklehurst, Department of Clinical Chemistry, Doncaster Royal Infirmary, UK.)... Figure 3.25 Starch gel electrophoresis of human serum proteins. Samples 1 and 2 are normal while samples 3, 4 and 5 show an extra band adjacent to the normal albumin which is due to the presence of bis-albumin. Sample 7 contains a myeloma protein that has remained near the origin. (Photograph by permission of Dr D. Brocklehurst, Department of Clinical Chemistry, Doncaster Royal Infirmary, UK.)...
Figure 11.13 Electrophoresis of human serum proteins. The electrophoretogram, after staining with a suitable dye, can be scanned using a densitometer, which gives a trace of the absorbance pattern of the strip. Figure 11.13 Electrophoresis of human serum proteins. The electrophoretogram, after staining with a suitable dye, can be scanned using a densitometer, which gives a trace of the absorbance pattern of the strip.
Figure 11.15 Immunoelectrophoresis of human serum proteins. The proteins are separated electrophoretically from wells cut in a suitable gel. After electrophoresis, a trough is cut in the gel parallel to the direction of migration and filled with an antiserum. The components are allowed to diffuse for 24-48 hours for precipitation lines to develop. Human serum contains many proteins, among which the immunoglobulins can be identified. Figure 11.15 Immunoelectrophoresis of human serum proteins. The proteins are separated electrophoretically from wells cut in a suitable gel. After electrophoresis, a trough is cut in the gel parallel to the direction of migration and filled with an antiserum. The components are allowed to diffuse for 24-48 hours for precipitation lines to develop. Human serum contains many proteins, among which the immunoglobulins can be identified.
Bone marrow aspirates and biopsy specimen from HIV-positive patients with plasmacytosis (T3) were analyzed to identify the pathologic correlates of polyclonal and monoclonal hypergammaglobulinemia in these patients. Serum protein electrophoresis and immunoelectrophoresis revealed monoclonal spikes in 25% of patients tested 75% of patient tests showed polyclonal hypergammaglobulinemia. [Pg.217]

Zone Electrophoresis in Starch Gels and Its Application to Studies of Serum Proteins O. Smithies... [Pg.390]

With the study of the migration of hydrogenium ions (H ) in a phenolphthalein gel by Lodge in 1886 and the description of the migration of ions in saline solutions by Kohlraush in 1897, a basis was set for the development of a new separation technique that we know today as electrophoresis. Indeed, several authors applied the concepts introduced by Lodge and Kohlraush in their methods and when Arne Tiselius reported the separation of different serum proteins in 1937, the approach called electrophoresis was recognized as a potential analytical technique. Tiselius received the Nobel Prize in Chemistry for the introduction of the method called moving boundary electrophoresis. ... [Pg.10]

Arne WK. Tiselius Sweden electrophoresis and serum proteins... [Pg.409]

PA McDonnell, GW Caldwell, JA Masucci. Using capillary electrophoresis/ frontal analysis to screen drugs interacting with human serum proteins. Electrophoresis 19 448-454 (1998). [Pg.85]

MG Quaglia, E Bossu, C DellAquila, M Guidotti. Determination of the binding of a /32-blocker drug, frusemide and ceftriaxone to serum proteins by capillary zone electrophoresis. J Pharm Biomed Anal 15 1033—1039, 1997. [Pg.249]

In 1956, Smithies and Poulik first used 2-DE combining paper and starch gel electrophoresis to separate serum proteins. Nearly 20 years later, polyacrylamide was applied as a support medium. Charge-based protein separation followed as isoelectric focusing (IEF), applied to SDS-PAGE. Later, urea and nonionic detergents were used in IEF-2DE. The most significant achievement was the separation of proteins from E. coli. [Pg.92]

TISEMIJS, ARNE W. K. (1902-1971). A Swedish biochemist who won the Nobel prize for chemistry in 1948, for his research on electrophoresis and adsorption analysis, especially for his discoveries concerning the complex nature of the serum proteins. His work also involved virus isolation and synthesis of blood plasma. He earned degrees from die University of Uppsala and Princeton University, as well as a multitude of honorary degrees. [Pg.1619]

Davis, B.J. 1964. Disc electrophoresis II Method and application to human serum proteins. Ann. N. Y. Acad. Sci. 121 404-427. [Pg.183]

Magi, B., Marzocchi, B., Bini, L., Cellesi, C., Rossolini, A., and Pallini, V. (1995) Two-dimensional electrophoresis of human serum proteins modified by ampicillin during therapeutic treatment. Electrophoresis 16, 1190-1192. [Pg.290]

High-resolution agarose gel electrophoresis of serum proteins can reveal the presence of a monoclonal immunoglobulin. The M band in the form of a tall, narrow spike and an intensely stained band can be found anywhere in the gamma,... [Pg.325]

Recently, the availability of capillary electrophoresis provides a sensitive method for enumerating the serum protein fractions without the use of staining and densitometric scanning because the electrophoretically separated fractions are quantitated by the measurement of UV absorbance. [Pg.326]

D6. de Wael, J., The combined influence of evaporation and diffusion on the separation of serum proteins by paper electrophoresis. In "Paper Electrophoresis Ciba Foundation Symposium (G. E. W. Wolstenholme and E. C. P. Millar, eds.), pp. 105-110. Churchill, London, 1956. [Pg.77]


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