Densitometric Evaluation of Microelectrophoretic Serum. Protein Patterns on Cellulose Acetate Membranes

1961 ◽  
Vol 33 (7) ◽  
pp. 860-861 ◽  
Author(s):  
B. W. Grunbaum ◽  
W. J. Fessel ◽  
C. F. Piel
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.


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.


1990 ◽  
Vol 55 (12) ◽  
pp. 2933-2939 ◽  
Author(s):  
Hans-Hartmut Schwarz ◽  
Vlastimil Kůdela ◽  
Klaus Richau

Ultrafiltration cellulose acetate membrane can be transformed by annealing into reverse osmosis membranes (RO type). Annealing brings about changes in structural properties of the membranes, accompanied by changes in their permeability behaviour and electrical properties. Correlations between structure parameters and electrochemical properties are shown for the temperature range 20-90 °C. Relations have been derived which explain the role played by the dc electrical conductivity in the characterization of rejection ability of the membranes in the reverse osmosis, i.e. rRO = (1 + exp (A-B))-1, where exp A and exp B are statistically significant correlation functions of electrical conductivity and salt permeation, or of electrical conductivity and water flux through the membrane, respectively.


Desalination ◽  
1985 ◽  
Vol 56 ◽  
pp. 251-260 ◽  
Author(s):  
M. Kurihara ◽  
W. Pusch ◽  
T. Tanaka

1977 ◽  
Vol 23 (1) ◽  
pp. 28-34 ◽  
Author(s):  
W H Siede ◽  
U B Seiffert

Abstract We present a new method for quantitative determination of alkaline phosphatase isoenzymes. This method consists of electrophoretic separation on cellulose acetate membranes, special fixation technique to avoid elution and diffusion of enzyme protein during incubation, specific staining, and quantitative evaluation by densitometric measurement. We highly recommend the precedure for routine clinical laboratory use. In all normal individuals we observe two isoenzymes of hepatic origin and one isoenzyme each of osseous, intestinal, and biliary origin. Quantitative normal values are presented. Precision of the method is calculated, the CV being less than 10%. The exactness of densitometric quantification is proved by comparison with kinetic assay of alkaline phosphatase isoenzymes by use of an elution method. Clinical implications of alkaline phosphatase isoenzymograms are reported and discussed in detail.


1959 ◽  
Vol 34 (177) ◽  
pp. 392-397 ◽  
Author(s):  
B. S. Kulkarni ◽  
R. S. Satoskar ◽  
M. N. Parikh ◽  
R. G. Chitre

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