A RAPID METHOD FOR FILTER PAPER ELECTROPHORESIS

A technique for filter paper electrophoresis and strip staining that permits the running time to be reduced to two hours or less is described. Some typical two hour electrophoretic patterns are illustrated and the clinical advantages of the technique mentioned. Details of a simple and inexpensive apparatus for electrophoresis on filter paper are given. Several variables affecting rapid and distinct protein separation, which were modified in the development of this method, and the relationships between these changes and the shortened running time are discussed.

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IMMUNOCHEMICAL STUDIES OF ANTITOXIN PRODUCED IN NORMAL AND ALLERGIC INDIVIDUALS HYPERIMMUNIZED WITH DIPHTHERIA TOXOID

Journal of Experimental Medicine ◽

10.1084/jem.100.5.485 ◽

1954 ◽

Vol 100 (5) ◽

pp. 485-495 ◽

Cited By ~ 6

Author(s):

William J. Kuhns

Keyword(s):

Filter Paper ◽

Booster Dose ◽

Paper Electrophoresis ◽

Hay Fever ◽

Diphtheria Toxoid ◽

Electrophoretic Patterns ◽

Electrophoretic Behavior ◽

Beta Globulin ◽

Before And After ◽

Serum Components

The method of filter paper electrophoresis was used to study proteins and protein-bound polysaccharides in sera obtained from subjects before and after a single booster dose of diphtheria toxoid, and in sera from allergic subjects. The electrophoretic patterns of precipitating antitoxic sera resembled those found in normal non-immune sera. However, skin-sensitizing antitoxic sera were distinguished by a relatively large beta globulin component and a small or indistinct alpha2 globulin. Fusion of both components was present in some sera containing this variety of antitoxin. Considerable amounts of serum-bound polysaccharides in these sera migrated relatively slowly in contrast to the behavior of polysaccharides of precipitating antitoxic sera which migrated faster when tested under similar conditions. Alterations in proteins and carbohydrates were most readily observed in specimens containing high titers of antitoxin. There were no demonstrable differences between the electrophoretic behavior of sera obtained from subjects before or after immunization with toxoid. Electrophoretic patterns of serum from allergic subjects who developed marked eosinophilia showed attenuation of the alphas globulin associated with a relative preponderance of slow migrating protein-bound polysaccharides. These alterations were not present in sera obtained from the same persons before and after the development of eosinophilia. Changes in the proteins and polysaccharides could not be demonstrated with consistency in subjects with mild to moderate hay-fever symptoms. One person who developed severe acute hay-fever symptoms showed alterations in the beta and alpha2 globulins. Rheumatic fever subjects showed no unusual changes in the distribution of serum components. However, transition from the acute process to convalescence is graphically demonstrated by the marked decreases in gamma and alpha globulins and in protein-bound carbohydrates.

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Cholesterol in Serum and Lipoprotein Fractions

Clinical Chemistry ◽

10.1093/clinchem/2.3.145 ◽

1956 ◽

Vol 2 (3) ◽

pp. 145-159 ◽

Cited By ~ 187

Author(s):

Joseph T Anderson ◽

Ancel Keys

Keyword(s):

Human Serum ◽

Total Cholesterol ◽

Filter Paper ◽

Room Temperature ◽

Paper Electrophoresis ◽

Cholesterol Content ◽

Intraindividual Variability ◽

Detailed Data ◽

The Stability ◽

Source Of Error

Abstract 1. Methods are described for the separation, by paper electrophoresis and by cold ethanol, of α- and β-lipoproteins in 0.1 ml. of serum, with subsequent analysis of cholesterol in the separated portions. 2. It is shown that both methods of separation yield separated fractions containing substantially the same amounts of cholesterol. 3. Detailed data are given on the errors of measurement for total cholesterol and for cholesterol in the separated lipoprotein fractions. 4. Studies are reported on the stability of cholesterol in stored serum and on paper electrophoresis strips. It is shown that simple drying on filter paper causes no change in cholesterol content and yields a product that is stable for many weeks at ordinary room temperature. 5. The sources of variability in human serum cholesterol values are examined and it is shown that spontaneous intraindividual variability is a much greater source of error than the errors of measurement with these methods.

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