scholarly journals Electrophoretic Profile of Serum Proteins Using Capillary Technique in Patients Attending the Douala General Hospital, Cameroon

2018 ◽  
Vol 6 (2) ◽  
pp. 50-55
Author(s):  
Judith Gwladys Ekwe Priso ◽  
Jean Pierre Nda Mefo’o ◽  
Cécile Okalla Ebongue ◽  
Eveline Ngouadjeu Dongho Tsakeu ◽  
Catherine Akono Ndi ◽  
...  
Keyword(s):  
Capillary Electrophoresis ◽  
General Hospital ◽  
Gel Electrophoresis ◽  
Serum Proteins ◽  
Agarose Gel Electrophoresis ◽  
Serum Samples ◽  
Electrophoretic Profile ◽  
Biuret Method ◽  
Accuracy Of Results ◽  
Separation Of Proteins

Background: Electrophoresis of serum proteins is an orientation examination routinely used in clinical practice. For a few years, agarose gel electrophoresis has tended to be replaced with capillary electrophoresis owing to an increase in the accuracy of results. However, this technique is uncommon and is not widely used in Cameroon. Objectives: The research aimed at studying the electrophoretic profile of serum proteins using capillary technique among patients attending the Douala General Hospital, Cameroon. Methods: Capillary electrophoresis was used to carry out tests on blood samples from any inpatients and outpatients and fasting for 8-12 hours. Capillary electrophoresis of serum samples was used for the separation of proteins into six fractions and the total protidemia of each serum samples was determined using the Biuret method. Results were interpreted by observing the shape of curves and quantitative variations in each fraction of the different serum proteins. Results: A total of 311 patients participated in the study. The sampled population aged 50±18 years on average and consisted of 55.3% men and 44.7% women. All capillary electrophoresis profiles presented six protein fractions, namely, albumin, alpha (1 and 2), beta (1 and 2) and gamma globulins. Pathological disorders were diagnosed in 290 patients and 21 patients had normal results. Inflammatory syndromes accounted for 63.34% and monoclonal gammopathies for 10.29% the main pathological disorder identified. Conclusion: Capillary electrophoresis provides a more precise identification of biological syndromes and clear distinction of the six fractions of each protein. Monoclonal profiles and inflammatory syndromes were well detected. A prevalence of 10.29% was determined for gammopathies.

scholarly journals Quantification of Serum Proteins Using Capillary Electrophoresis

1995 ◽  
Vol 32 (5) ◽  
pp. 493-497 ◽  
Author(s):  
M A Jenkins ◽  
M D Guerin
Keyword(s):  
Capillary Electrophoresis ◽  
Gel Electrophoresis ◽  
Serum Proteins ◽  
Clinical Laboratory ◽  
Charged Particles ◽  
Protein Electrophoresis ◽  
Agarose Gel Electrophoresis ◽  
Serum Samples ◽  
Routine Clinical Laboratory ◽  
Sample Dilution

Capillary electrophoresis is a technique that can be automated for the separation of charged particles. By investigating suitable sample dilution and injection time and adhering to a strict washing procedure we have been able to quantify paraproteins in serum samples. This has enabled us to use the technique of capillary electrophoresis for the provision of serum protein electrophoresis in a routine clinical laboratory. We present our findings of 260 serum samples, which included 76 samples with paraproteins analysed by both capillary electrophoresis (EC) and high resolution agarose gel electrophoresis (HRAGE). CE was able to detect all the monoclonal bands detected by HRAGE, and, in particular, better able to detect IgA monoclonal bands occurring in the beta region. The major advantages of CE over HRAGE relate to the automated nature of CE with the elimination of the need for a densitometer.

Quantitative analysis of serum proteins separated by capillary electrophoresis

1993 ◽  
Vol 39 (4) ◽  
pp. 689-692 ◽  
Author(s):  
J W Kim ◽  
J H Park ◽  
J W Park ◽  
H J Doh ◽  
G S Heo ◽  
...  
Keyword(s):  
Capillary Electrophoresis ◽  
Gel Electrophoresis ◽  
Serum Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis ◽  
Serum Samples ◽  
Polyclonal Gammopathy ◽  
Quantitative Analyses

Abstract The possibility of open tubular capillary electrophoresis for clinical diagnostic use is examined. Capillary electrophoresis was performed in an untreated 50 microns (i.d.) x 100 cm (65 cm to detector) capillary with detection of absorbance at 200 nm. Conditions for the separation of serum proteins without adsorption to the capillary surface were established. Quantitative analyses of serum samples from 38 patients with liver cirrhosis, nephrotic syndrome, or polyclonal gammopathy by capillary electrophoresis were done and the results were compared with those by conventional agarose gel electrophoresis and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. All samples were analyzed in duplicate. We evaluated linearity of response, within-run CV, and the correlation between capillary electrophoresis and agarose gel electrophoresis.

scholarly journals Detection and identification of monoclonal gammopathies by capillary electrophoresis

1998 ◽  
Vol 44 (6) ◽  
pp. 1184-1190 ◽  
Author(s):  
Yvonne Henskens ◽  
John de Winter ◽  
Maurits Pekelharing ◽  
Gabrielle Ponjee
Keyword(s):  
Capillary Electrophoresis ◽  
Gel Electrophoresis ◽  
Good Alternative ◽  
The Other ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis ◽  
Routine Method ◽  
Serum Samples ◽  
Detection And Identification ◽  
Immunofixation Electrophoresis

Abstract Capillary electrophoresis (CE) and immunosubtraction capillary electrophoresis (IS-CE) were compared with the conventional methods agarose gel electrophoresis (AGE) and immunofixation electrophoresis (IFE) for detection and identification of paraproteins. In total, 74 paraproteins out of 468 serum samples were detected by both methods. Seventy-three monoclonal bands with concentrations ranging from 0.6 to 50.9 g/L were detected by the routine method. With CE, 70 paraproteins were detected and quantified on the electropherogram. Four paraproteins were not detected by CE; three of these were IgG (0.6, 1.1, and 2.2 g/L, respectively), and one was a IgM paraprotein (20.3 g/L) that could be visualized by minor changes in the running conditions. In comparison with IFE, 69 paraproteins were typed identically using IS-CE; only one paraprotein (IgMκ, 14.9 g/L) could not be identified. On the other hand, a monoclonal IgA band that had not been detected by AGE was identified by CE and IS-CE. We conclude that, in general, CE could be a useful method for detection of paraproteins and that IS-CE is a good alternative to IFE. Additional studies are required to investigate the ionic strength and pH of the running buffer, because these prove to be the most crucial factors for routine CE separation of paraproteins.

scholarly journals Computer-supported Detection of M-Components and Evaluation of Immunoglobulins after Capillary Electrophoresis

2001 ◽  
Vol 47 (1) ◽  
pp. 110-117 ◽  
Author(s):  
Magnus Jonsson ◽  
Joyce Carlson ◽  
Jan-Olof Jeppsson ◽  
Per Simonsson
Keyword(s):  
Capillary Electrophoresis ◽  
Decision Support ◽  
Protein Separation ◽  
Serum Proteins ◽  
Cost Effective ◽  
Clinical Samples ◽  
Serum Samples ◽  
Computerized Decision Support ◽  
Cost Effective Method ◽  
Mathematical Algorithms

Abstract Background: Electrophoresis of serum samples allows detection of monoclonal gammopathies indicative of multiple myeloma, Waldenström macroglobulinemia, monoclonal gammopathy of undetermined significance, and amyloidosis. Present methods of high-resolution agarose gel electrophoresis (HRAGE) and immunofixation electrophoresis (IFE) are manual and labor-intensive. Capillary zone electrophoresis (CZE) allows rapid automated protein separation and produces digital absorbance data, appropriate as input for a computerized decision support system. Methods: Using the Beckman Paragon CZE 2000 instrument, we analyzed 711 routine clinical samples, including 95 monoclonal components (MCs) and 9 cases of Bence Jones myeloma, in both the CZE and HRAGE systems. Mathematical algorithms developed for the detection of monoclonal immunoglobulins (MCs) in the γ- and β-regions of the electropherogram were tested on the entire material. Additional algorithms evaluating oligoclonality and polyclonal concentrations of immunoglobulins were also tested. Results: CZE electropherograms corresponded well with HRAGE. Only one IgG MC of 1 g/L, visible on HRAGE, was not visible after CZE. Algorithms detected 94 of 95 MCs (98.9%) and 100% of those visible after CZE. Of 607 samples lacking an MC on HRAGE, only 3 were identified by the algorithms (specificity, 99%). Algorithms evaluating total gammaglobulinemia and oligoclonality also identified several cases of Bence Jones myeloma. Conclusions: The use of capillary electrophoresis provides a modern, rapid, and cost-effective method of analyzing serum proteins. The additional option of computerized decision support, which provides rapid and standardized interpretations, should increase the clinical availability and usefulness of protein analyses in the future.

Evaluation of usefulness of a commercial agarose gel electrophoresis kit (QuickGel SP) for bovine serum protein electrophoresis

2017 ◽  
Vol 20 (3) ◽  
pp. 527-534
Author(s):  
Y. Okatsu ◽  
N. Yamagishi ◽  
K. Hatate ◽  
B. Devkota
Keyword(s):  
Serum Protein ◽  
Gel Electrophoresis ◽  
Bovine Serum ◽  
Protein Fractions ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis ◽  
Serum Samples ◽  
Cellulose Acetate Electrophoresis ◽  
Γ Globulins ◽  
Bovine Serum Protein

Abstract The aim of this study was to show the usefulness of a commercial agarose gel electrophoresis (AGE) kit (QuickGel SP) for separating bovine serum protein fractions in comparison with conventional cellulose acetate electrophoresis (CAE). Serum protein bands were verified using five reference reagents corresponding to albumin and α1-, β1-, β2-, and γ-globulins. AGE clearly revealed six separated fractions of albumin and α1-, α2-, β1-, β2-, and γ-globulin fractions in 100% and 77.8% in serum samples of dairy cows from the healthy (n=27) and diseased groups (n=27), respectively. The α1- and α2-globulins were not separated by CAE in 14.8% and 96.3% of the samples from the healthy and diseased groups, respectively, whereas β2- and γ-globulin were not separated by CAE in 96.3% and 100% of the samples from the healthy and diseased groups, respectively. More than 94% of the points for the α-globulin fractions (α1- and α2-globulins), the β-γ-globulin fractions (β1-, β2-, and γ-globulins), and the albumin/globulin ratio between AGE and CAE were within agreement on the Bland-Altman plots. However, the mean biases were not near zero in the albumin and β-γ-globulin fractions. These results suggest that the high-resolution commercial AGE kit can be utilized to separate bovine serum protein fractions.

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