scholarly journals Clinical significance of serum protein electrophoretic fractionation by cellulose acetate electrophoresis

1977 ◽  
Vol 21 (3) ◽  
pp. 159-167
Author(s):  
Tadashi Kawai
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.


1965 ◽  
Vol 11 (10) ◽  
pp. 937-942 ◽  
Author(s):  
Alex Kaplan ◽  
John Savory

Abstract A rapid system for the quantitative fractionation of serum proteins by electrophoresis on cellulose-acetate membranes was evaluated and found to be quite precise. The reproducibility (coefficient of variation) of the routine fractionation of a control serum carried out 40 times during a 15-week period was 2.4% for albumin and 14.2, 6.0, 6.1, and 5.2%, respectively, for the α1-, α2-, β-, and γ-globulin fractions. Normal values are given for serum protein fractions (specimens from nonprofessional blood donors) obtained by cellulose acetate electrophoresis.


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.


1967 ◽  
Vol 18 (5) ◽  
pp. 821 ◽  
Author(s):  
C Dobson

The serum proteins of worm-free crossbred lambs were found to vary over a period of 10 weeks. Infestation of these lambs with 2000 infective Oesophagostomum columbianum larvae also caused marked changes in various serum proteins separated by cellulose acetate electrophoresis. The total serum proteins of infested sheep remained static or decreased slightly over the period of observation. There was a marked hypoalbuminaemia (measured in grams per cent.) in the infested lambs. The α-globulin retained the same level as in the controls; this was attributed to compensatory synthesis to overcome the osmotic changes produced by albumin loss. The ß1-globulin decreased throughout infestations; both albumin and ß1-globulin could have been lost through inflammation of the alimentary tract. The ß2-globulin increased very greatly during infestation; this was attributed to an immunological response. The y-globulin level at first decreased, but after 10 days the level increased at a rate commensurate with that in the control lambs. This increase was also attributed to an immunological response.


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.


1984 ◽  
Vol 3 (4) ◽  
pp. 317-321
Author(s):  
H. J. Esber ◽  
P. Zavorskas ◽  
H. Rosenkrantz

It was of interest, in the absence of such data, to investigate the effects of x-irradiation on individual serum proteins, including immunoglobulin G. Doses of 600 and 800 rads to the abdominal areas of immature beagles were sufficient to evoke emesis and hemorrhages of lymph nodes and perilobular areas of the liver. Seven days after irradiation of 8–12 male dogs/dose, serum specimens were analyzed by cellulose acetate electrophoresis and radial immunodiffusion. Radiation reduced serum protein and albumin by 12%, β2 by 27%, γ-globulin by 19%, and IgG by 35%, while increasing α2 by 50%. These results are in conformity with the radiation damage to lymph nodes (IgG decrease) and liver (plasma protein fall) and initiation of the inflammatory process (α2 rise).


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