scholarly journals On the standard procedure for the analysis of serum protein fractions by cellulose acetate electrophoresis

1966 ◽  
Vol 11 (4) ◽  
pp. 351-356
Author(s):  
Y. Ogawa ◽  
M. Abe ◽  
M. Kitamura ◽  
N. Kosakai ◽  
K. Shimao ◽  
...  
1986 ◽  
Vol 32 (2) ◽  
pp. 356-357 ◽  
Author(s):  
S N Kahn ◽  
L P Strony

Abstract We studied the precision of densitometric quantification of the protein zones resolved by cellulose acetate electrophoresis. Replicate analyses of patients' samples by a single technologist showed mean CVs ranging from 2.9% for serum albumin to 9.5% for alpha 1-globulin. There were marked differences in measurements obtained by replicate analysis of the same samples by two experienced technologists. We calculated what changes in fractional concentrations would be analytically significant and concluded that densitometry of cellulose acetate electrophoretograms can only be semi-quantitative. We suggest that visual interpretation of high-resolution electrophoretic patterns by a trained observer can replace densitometry in most cases.


1972 ◽  
Vol 18 (12) ◽  
pp. 1541-1542 ◽  
Author(s):  
J W Keyser ◽  
G L Watkins

Abstract We have evaluated results for albumin obtained by a standard procedure for cellulose acetate electrophoresis of proteins in serum. The Ponceau S-stained albumin and globulins were eluted and the albumin was calculated by the generally accepted formula [(albumin-bound dye absorbance/absorbance of total protein-bound dye) x total serum protein concn] and by the formula (absorbance of albumin-bound dye in test/absorbance of albumin-bound dye in a reference serum) x concn of albumin in reference serum. The ratio of values by the first and second methods ranged from 0.93 to 1.30, the first giving the higher results in cases of discrepancy. These findings confirm the limitations in accurately calculating any serum-protein fraction by the first method. The second method appears to be the more accurate.


1963 ◽  
Vol 9 (3) ◽  
pp. 317-324 ◽  
Author(s):  
Raymond C Bartlett

Abstract A method of electrophoresis utilizing cellulose acetate is described wherein quantitation of serum protein fractions by densitometry is accomplished within 2 hr. of initiation of the procedure. The densitometer was found to have a linear response to amido black dye. Albumin and γ-globulin demonstrated equal dye-binding characteristics. Combined with the absence of albumin trailing, this has afforded excellent quantitations of serum protein fractions.


1970 ◽  
Vol 16 (5) ◽  
pp. 416-419 ◽  
Author(s):  
Rita M Windisch ◽  
Mark M Bracken

Abstract A membrane ultrafiltration system is described and evaluated for rapidly concentrating cerebrospinal fluid before cellulose acetate electrophoresis. Results with this system were compared with those obtained by use of vacuum ultrafiltration through a collodion sac. Mean values for the various protein fractions were determined for normal cerebrospinal fluid. The results, in percentage of total protein, after membrane and vacuum ultra-filtration concentration were, respectively: 3.8 and 5.2% prealbumin, 65.5 and 63.9% albumin, 3.6 and 3.6% ∝1-globulin, 6.8 and 6.1% arglobulin, 12.4 and 12.9% a-globulin, and 7.6 and 8.2% γ-globulin.


2017 ◽  
Vol 20 (3) ◽  
pp. 527-534
Author(s):  
Y. Okatsu ◽  
N. Yamagishi ◽  
K. Hatate ◽  
B. Devkota

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.


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.


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