scholarly journals ELECTROPHORESIS OF PROTEINS ON FILTER PAPER

1951 ◽  
Vol 35 (1) ◽  
pp. 89-118 ◽  
Author(s):  
Henry G. Kunkel ◽  
Arne Tiselius
Keyword(s):  
Serum Albumin ◽  
Filter Paper ◽  
Serum Proteins ◽  
Paper Electrophoresis ◽  
Normal Serum ◽  
Concentration Gradients ◽  
Simplified Procedure ◽  
Highly Porous ◽  
Electrophoresis Of Proteins ◽  
Serum Components

A simplified procedure for filter paper electrophoresis is described in which disturbing factors such as evaporation, heating, buffer concentration gradients, and pH changes in the electrode vessels were reduced to a minimum. Artificial mixtures of highly purified proteins could be separated and the components isolated. The application of the method to a variety of studies on serum proteins is demonstrated. Protein concentration in paper segments was determined by two different methods of protein estimation. Curves were obtained showing the same five major peaks for normal serum as found by the classical methods of free electrophoresis. Comparisons were made of the areas of the various components under the curves obtained with the different methods. Two dimensional electrophoresis was applied to serum and serum components. It proved of value in demonstrating the heterogeneity of fractions such as the γ-globulin of serum. The polysaccharide dextran was used as an index of the extent of electro-osmotic flow during the course of the various experiments. The ratio of the distance of electroosmotic flow and the distance of protein migration was shown to be constant for a given type of paper. For serum albumin on Munktell 20 paper this ratio was 0.35. A formula for mobilities applicable to liquid in a highly porous supporting medium is presented. Mobility values for human serum albumin at various pH levels on paper showed approximate agreement with those obtained in free solution giving a similar isoelectric point.

BIOCOLLOIDS IN NORMAL HUMAN URINE: I. AMOUNT AND ELECTROPHORETIC CHARACTERISTICS

1958 ◽  
Vol 36 (1) ◽  
pp. 1159-1166 ◽  
Author(s):  
T. Webb ◽  
B. Rose ◽  
A. H. Sehon
Keyword(s):  
Human Serum ◽  
Electrophoretic Mobility ◽  
Human Urine ◽  
Filter Paper ◽  
Radioactive Iodine ◽  
Normal Serum ◽  
Γ Globulins ◽  
Normal Human ◽  
Normal Urine ◽  
Serum Components

The biocolloids of normal urine have been isolated and characterized by free electrophoresis and electrophoresis on filter paper. An average of 133 mg of material was recovered from 24-hour aliquots of normal urine. This material was composed of at least seven components as revealed by free electrophoresis at pH 8.6. Five of these components were similar in electrophoretic mobility to the five serum components. A relatively large amount of material was present which behaved like the acid mucoproteins of normal serum. No lipoproteins were detected. Some of the components of the urinary biocolloids were shown to be derived from human serum γ-globulins by labelling the latter with radioactive iodine.

Filter Paper Electrophoresis of Serum Proteins from Sharks

Copeia ◽  
1957 ◽  
Vol 1957 (4) ◽  
pp. 292 ◽  
Author(s):  
Theodore J. Starr ◽  
Walter Fosberg
Keyword(s):  
Filter Paper ◽  
Serum Proteins ◽  
Paper Electrophoresis

scholarly journals Studies in Bisalbuminemia: Binding Properties of the Two Albumins

Blood ◽  
1962 ◽  
Vol 20 (2) ◽  
pp. 156-164 ◽  
Author(s):  
EDWARD J. SARCIONE ◽  
C. WILLIAM AUNGST
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Protein ◽  
Serum Proteins ◽  
Protein Pattern ◽  
Total Serum ◽  
Binding Properties ◽  
Normal Human ◽  
Serum Components

Abstract 1. An abnormal serum protein pattern in a patient with Wegener’s granulomatosis and five of his relatives was identified as bisalbuminemia by electrophoretic and immunochemical methods. 2. With the exception of the patient with Wegener’s syndrome, the presence of bisalbuminemia was not associated with a significant change in total serum proteins, total albumin, serum components other than albumin, or any disease. 3. Addition of I131-thyroxine to bisalbumin sera resulted in thyroxine binding by albumin B but not by albumin A. The failure of albumin A to bind added I131-thyroxine leads to speculation that, in this family, neither albumin A nor B are identical to normal human serum albumin.

FILTER PAPER ELECTROPHORESIS OF SERUM PROTEINS IN CLINICAL PRACTICE

1954 ◽  
Vol 3 (4) ◽  
pp. 270-278 ◽  
Author(s):  
E. G. MCQUEEN ◽  
R. F. O'SHEA ◽  
M. P. SUMMERFIELD
Keyword(s):  
Clinical Practice ◽  
Filter Paper ◽  
Serum Proteins ◽  
Paper Electrophoresis

scholarly journals THE OCCURRENCE DURING ACUTE INFECTIONS OF A PROTEIN NOT NORMALLY PRESENT IN THE BLOOD

1941 ◽  
Vol 73 (2) ◽  
pp. 183-190 ◽  
Author(s):  
Colin M. MacLeod ◽  
Oswald T. Avery
Keyword(s):  
Serum Albumin ◽  
Acute Phase ◽  
Sodium Sulfate ◽  
Serum Proteins ◽  
Tap Water ◽  
Normal Serum ◽  
Reactive Protein ◽  
Acute Infections ◽  
Acute Phase Serum

Methods are described for isolating a protein commonly present in the blood of patients during the acute phase of various infections which, unlike the normal serum proteins, is precipitable by the C polysaccharide of Pneumococcus. The reactive protein is present in the fraction of serum albumin precipitated by either ammonium or sodium sulfate between 50 and 75 per cent saturation. From this fraction the reactive protein separates out on dialysis against tap water. Following removal of the alcohol-ether-soluble lipids from acute phase serum the reactive protein becomes soluble in tap water, and is no longer precipitable by traces of calcium but still retains its precipitability with the C polysaccharide.

STUDIES ON THE LIVETINS OF HEN'S EGG YOLK: II. IMMUNOELECTROPHORETIC IDENTIFICATION OF LIVETINS WITH SERUM PROTEINS

1964 ◽  
Vol 42 (8) ◽  
pp. 1119-1131 ◽  
Author(s):  
Chi-Ching Mok ◽  
R. H. Common
Keyword(s):  
Serum Albumin ◽  
Filter Paper ◽  
Laying Hens ◽  
Serum Proteins ◽  
Egg Yolk ◽  
Laying Hen ◽  
Immunoelectrophoretic Analysis ◽  
Hen’S Egg ◽  
Additional Antigen ◽  
Serum Antigens

Ten antigens have been distinguished in the sera of cocks and non-laying hens by immunoelectrophoretic analysis (IEA) against homologous rabbit antisera. An additional antigen has been found in the sera of laying hens by IEA against anti-laying-hen serum.Four of the serum antigens obtained by IEA have been correlated electrophoretically with the filter paper electrophoretic fractions serum albumin, serum α2-globulin, serum β-globulin, and serum γ-globulin.Serum albumin, serum α1-globulin, serum β-globulin, and serum γ-globulin have been identified immunologically with alpha-livetin, a livetin antigen (livetin 2), gamma1-livetin and gamma2-livetin respectively. Another antigen of cock serum and hen serum has been identified by IEA with a livetin antigen detected by IEA of livetin against anti-cock, anti-hen, and anti-yolk sera.

THE DETERMINATION OF SERUM PROTEIN FRACTIONS ON FILTER PAPER ELECTROPHEROGRAMS BY THE BIURET REACTION, AND SOME OBSERVATIONS ON THE SERUM PROTEINS OF THE ESTROGENIZED IMMATURE PULLET

1954 ◽  
Vol 32 (1) ◽  
pp. 189-199 ◽  
Author(s):  
W. P. McKinley ◽  
W. A. Maw ◽  
W. F. Oliver ◽  
R. H. Common
Keyword(s):  
Serum Protein ◽  
Filter Paper ◽  
Domestic Fowl ◽  
Serum Proteins ◽  
Paper Electrophoresis ◽  
Protein Fractions ◽  
Veronal Buffer

An application of the biuret reaction to the determination of protein fractions on filter paper electropherograms of serum is described. The relative mobilities of the serum protein fractions of the domestic fowl and of man are compared. Values are reported for serum protein fractions as separated by filter paper electrophoresis in a methanolic veronal buffer. Some observations on the serum proteins of the estrogenized immature pullet are reported; and it is tentatively suggested that another fraction as well as serum phosphoprotein appears in the serum of the pullet as a consequence of treatment with estrogen.

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

1954 ◽  
Vol 100 (5) ◽  
pp. 485-495 ◽  
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.

Filter-Paper Electrophoresis of Serum Proteins from Small Animals

1953 ◽  
Vol 26 (2) ◽  
pp. 95-100 ◽  
Author(s):  
Thomas L. Gleason ◽  
Felix Friedberg
Keyword(s):  
Filter Paper ◽  
Serum Proteins ◽  
Paper Electrophoresis ◽  
Small Animals
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