Clinical usefulness of the molecular interpretation of the cellulose acetate serum protein electrophoresis

1980 ◽  
Vol 10 (1) ◽  
pp. 239-242
Author(s):  
Francesco Aguzzi ◽  
Concetta Petrini ◽  
Silvia Perolini ◽  
Gian Paolo Merlini ◽  
Marisa Maggi ◽  
...  
1987 ◽  
Vol 33 (1) ◽  
pp. 182-184 ◽  
Author(s):  
F J Liu ◽  
H A Fritsche ◽  
J M Trujillo

Abstract Our study of 95 serum samples from 37 patients with monoclonal gammopathy revealed distorted irregular monoclonal (M) protein bands after serum protein electrophoresis (SPE) on cellulose acetate membrane. In 71 (75%) of the 95 sera, the M-protein was underestimated and the albumin concentration overestimated. Dilution of the serum sample before SPE eliminated the abnormality of the M-protein bands. By SPE, the mean albumin concentration in these 71 undiluted sera was 45.8 (SD 7.4) g/L vs 37.9 (SD 5.8) g/L for the diluted sera; moreover, this was true of individual samples: measured albumin concentration in each diluted serum sample was always less than in the undiluted serum. As measured by the bromcresol green dye-binding method, the albumin concentration was 32.8 (SD 5.9) g/L. Similarly, the M-protein concentration in SPE was 49.5 (SD 12.3) g/L for the undiluted sera vs 61.8 (SD 15.1) g/L for the diluted sera, and the M-protein concentration in each diluted serum sample always exceeded that in the undiluted serum. Underestimation of M-protein limits the usefulness of M-protein measurement in evaluating the patient's response to therapy and for early detection of disease progression. SPE strips should be carefully inspected visually, and sera with M-protein band abnormalities should be diluted and re-assayed if SPE is to quantify concentrations of M-protein and albumin accurately.


1970 ◽  
Vol 16 (9) ◽  
pp. 760-762 ◽  
Author(s):  
Sylvan M Sax ◽  
John J Moore

Abstract A computer program has been written for off-line calculation of relative and absolute percentages of the five serum protein fractions usually seen on cellulose acetate electrophoretograms, with use of manually observed peak heights on densitometer scans. With myeloma-like peaks, both peak height and width at half-peak height must be measured. Routine application of the program saves technician time and decreases the number of large random errors.


1991 ◽  
Vol 35 (1) ◽  
pp. 15-20
Author(s):  
Yoshiko Hirose ◽  
Katuichi Sasaki ◽  
Yasuko Yamagishi ◽  
Ikunosuke Sakurabayashi ◽  
Tadashi Kawai

1969 ◽  
Vol 15 (4) ◽  
pp. 271-281 ◽  
Author(s):  
M H Gault ◽  
S Hsieh ◽  
E Elzer

Abstract The concentrations of serum immunoglobulins (Ig) G, A, and M were correlated with specific features in the β-γ region of densitometer patterns of serum protein electrophoresis on cellulose acetate membranes; visual analysis of densitometer patterns permitted semiquantitative prediction of values for IgG and IgA. Important immunoglobulin abnormalities, particularly elevations of IgA, were seen in some cases even when normal values were obtained from analyses of electrophoresis by usual densitometer integrator technics; many such instances were detectable by inspection of the densitometer tracing.


1980 ◽  
Vol 26 (8) ◽  
pp. 1221-1223 ◽  
Author(s):  
J Ambler ◽  
M Rodgers

Abstract Two new non-barbiturate buffers have been formulated for serum protein electrophoresis on cellulose acetate membranes. Both buffers give five distrinct fractions and are suitable for all systems, but have been primarily designed to meet the needs of the Gelman "Sepratek" system. One buffer is a tris(hydroxymethyl)aminomethane (Tris)/hippurate formulation; the other is composed of Tris/N-[tris(hydroxymethyl)methyl]glycine (Tricine)/sodium chloride/sodium salicylate. Both buffers allow reliable quantitation of protein fractions, giving results that correlated well with those obtained from barbiturate separations. The major advantage of these buffers is that they do not contain drugs of abuse.


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