Concentration of Cerebrospinal Fluid Proteins and Their Fractionation by Cellulose Acetate Electrophoresis

1966 ◽  
Vol 12 (10) ◽  
pp. 717-727 ◽  
Author(s):  
Alex Kaplan ◽  
Murray Johnstone

Abstract Various technics for concentrating cerebrospinal fluid (CSF) prior to electrophoretic separation of the protein fractions were tested. Vacuum ultrafiltration through a collodion sac proved to be the most reliable and convenient method. The proteins in the concentrate were separated by cellulose acetate electrophoresis and quantitated densitometrically. The mean values for the various protein fractions in normal CSF were the following: 4.9% pre-albumin, 61.5% albumin, 4.5% α1 globulin, 6.7% α2 globulin, 13.7% β globulin, and 8.8% γ globulin.

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.


Author(s):  
ALEX KAPLAN ◽  
JOHN SAVORY ◽  
WILLARD R. FAULKNER ◽  
GUILFORD G. RUDOLPH ◽  
WENDELL J. FORD ◽  
...  

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.


1982 ◽  
Vol 28 (1) ◽  
pp. 180-182 ◽  
Author(s):  
H Cloppet ◽  
A Francina ◽  
H Coquelin ◽  
Y Boucaud-Maître ◽  
P Hutinel ◽  
...  

Abstract We evaluated nephelometers from Behring, Hyland, and Beckman for IgG, IgA, and IgM quantitation in sera from patients with monoclonal gammopathies. The intra-batch precision of each instrument for each immunoglobulin class and for different concentrations of the same immunoglobulin was compared to the one obtained with the radial immunodiffusion method. No nephelometer showed a clearly better precision. The correlation with cellulose acetate electrophoresis was good for each of the three nephelometers. The mean value by the radial immunodiffusion method was higher than corresponding determinations by nephelometry.


1969 ◽  
Vol 47 (4) ◽  
pp. 455-460 ◽  
Author(s):  
M. E. Kiely ◽  
E. L. Tan ◽  
T. Wood

Transketolase (EC 2.2.1.1) was purified 12-fold from an extract of dried Candida utilis by two fractionations with acetone followed by chromatography on DEAE-Sephadex. The fractions from the column were free from D-ribose 5-phosphate ketol isomerase and D-ribulose 5-phosphate 3-epimerase and could be used for the assay of D-xylulose 5-phosphate and of the epimerase. Three peaks of transketolase activity were eluted from the chromatography column; the material from each peak had a Michaelis constant for D-xylulose 5-phosphate close to the mean value for the three peaks of 6.8 × 10−5 M and gave the same two-banded pattern on cellulose acetate electrophoresis. When transaldolase was present in the material placed on the column, it appeared with transketolase in each of the three peaks. The enzyme could be stored for several months, in solution frozen at −20°. Dialysis against water caused a loss of activity which could be restored by the addition of thiamine pyrophosphate. The enzyme catalyzed the condensation of hydroxypyruvate with D-glyceraldehyde phosphate to form D-xylulose 5-phosphate.


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.


1980 ◽  
Vol 14 (1) ◽  
pp. 41-42 ◽  
Author(s):  
Rodney K. Kusumi ◽  
Joseph F. Plouffe

In 35 normal rabbits the cerebrospinal fluid glucose values ranged between 56 and 135 mg/dl, mean and standard deviation 78 ± 13 mg/dl. Cerebrospinal total protein values ranged from 16 to 66 mg/dl, mean and standard deviation 33 ± 10 mg/dl. The mean values were similar to those reported for human cerebrospinal fluid. Depression of the cerebrospinal glucose level in the rabbit may parallel the human situation and prove to be a useful marker of purulent inflammation.


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