Electrophoresis of serum globulin

Tiselius, Arne

doi:10.1042/bj0311464

Cited by 303 publications

(54 citation statements)

References 7 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The order of migration of the chief protein fractions of human plasma in buffers at pH 7.7 is albumin, a-globulin, f8-globulin, fibrinogen and y-globulin. These boundaries were first noted in horse serum by Tiselius (7), later in human plasma by Stenhagen (8).…”

Section: Methodsmentioning

confidence: 99%

Electrophoretic Analysis of the Proteins of Plasma and Serous Effusions

Luetscher

1941

J. Clin. Invest.

104

View full text Add to dashboard Cite

The basic characteristics of serous effusions are well established. The matrix of water and salt is nearly identical with that of blood (1, 2). The cells, derived from blood or from tissues in contact with the effusion, vary widely in type and number. The protein content also varies within wide limits, and the specific gravity of the fluid with it (3, 4, 5).Serous effusions are classically divided into "transudates " and " exudates," implying different mechanisms of formation. The transudate is supposed to be produced by mechanical factors, such as change in hydrostatic or colloid osmotic pressure, while the exudate is produced by the reaction of the serous membrane to the presence of bacteria or noxious substances. Practically, the differentiation is made on the specific gravity, the cell count, and the presence or absence of clotting. This division is very useful, but shows some defects on closer examination. Not infrequently the distinction is difficult to make with the fluid in hand, as the white cell count and the specific gravity are not dearly in one class or another, the dividing line being ill-defined. Also, there is no place in the classification for fluids of neoplastic origin.In an attempt to evaluate the factors involved in the production of serous effusions and to determine the presence or absence of a sharp distinction between the various types of fluid, the proteins of the fluids have been studied by electrophoresis and compared with the proteins of the blood in each case.Blood proteins vary both in size and in net charge. Rate of migration in an electric field depends on both of these factors and allows the differentiation into more fractions than can be clearly detected by fractional precipitation by neutral salts or by ultracentrifugal analysis. This method also has the advantage of an accuracy greater than that of the so-called salting-out methods ( 11 ) and permits the quantitative estimation of albumin, fibrinogen and the three chief globulin fractions. METHODSThe electrophoresis apparatus of Tiselius was used (6). Plasma is layered in the lower half of the U-tube under buffer, against which the plasma has previously been dialyzed. Direct 1. Normal blood. The order of migration of the chief protein fractions of human plasma in buffers at pH 7.7 is albumin, a-globulin, f8-globulin, fibrinogen and y-globulin. These boundaries were first noted in horse serum by Tiselius (7), later in human plasma by Stenhagen (8).Concerning the proportions of these fractions in human plasma and serum, there is excellent 99

show abstract

Section: Methodsmentioning

confidence: 99%

Electrophoretic Analysis of the Proteins of Plasma and Serous Effusions

Luetscher

1941

J. Clin. Invest.

104

View full text Add to dashboard Cite

show abstract

“…With this apparatus he has studied, among other things, the proteins of horse serum (5,6). The simplicity of the method, the sharp separation of the fractions, and the small amounts of material required combine to make it an excellent procedure for the study of human proteins.…”

mentioning

confidence: 99%

Electrophoretic Analysis of Plasma and Urinary Proteins

Luetscher

1940

J. Clin. Invest.

168

View full text Add to dashboard Cite

“…The affinity of serum albumin to various chemical dyes and to bilirubin has been observed previously (32,33,11) and further investigations of the binding capacities of the various serum components will prove very instructive. In mixtures of Hp and isolated proteins such as egg albumin, globulin gamma, or Felton solution, however, the Hp migrates independently and can be entirely dissociated from the proteins, if runs are continued sufficiently long.…”

Section: Discussionmentioning

confidence: 99%

“…Separation of the protein fractions of anti-egg albumin rabbit serum was carried out in the electrophoresis apparatus of Tiselius (9)(10)(11)(12).…”

mentioning

confidence: 99%

Studies on Photo-Oxidation of Antigen and Antibodies

Smetana

Shemin

1941

Journal of Experimental Medicine

View full text Add to dashboard Cite

1. Quantitative precipitin studies indicate that progressive photo-oxidation progressively destroys the antigenic function of egg albumin. 2. Quantitative precipitin reactions of antisera (anti-egg albumin rabbit serum and antipneumococcus Type I horse serum) demonstrate that progressive photo-oxidation causes progressive lowering of the potency of the sera. 3. Quantitative precipitin reactions of the photo-oxidized globulin gamma fraction of anti-egg albumin rabbit serum and of Felton solution of antipneumococcus Type I horse serum show that these specific antibody fractions behave similarly to antibodies in whole sera. 4. Egg albumin whose precipitin reaction is destroyed by photo-oxidation no longer causes anaphylaxis in guinea pigs and does not produce precipitins in rabbits. 5. Chemical studies of progressively photo-oxidized egg albumin show a progressive destruction of tryptophane and histidine while tyrosine remains intact and cystine is reversibly oxidized. Sulfhydryl groups can no longer be demonstrated in photo-oxidized egg albumin whose antigenic characteristics are greatly weakened. 6. Similar studies on the globulin gamma fraction of anti-egg albumin rabbit serum and on Felton solution show no diminution of these amino acids in photo-oxidized material whose antigenic properties are destroyed. 7. The non-coagulable nitrogen and the amino nitrogen of egg albumin, antisera, and their specific antibody fractions show but an insignificant increase during photo-oxidation, indicating that the loss of the precipitin reaction is not due to splitting of the respective protein molecules. 8. Electrophoretic studies of egg albumin, antisera, and their specific antibody fractions show that photo-oxidation causes a marked alteration of the pattern of these substrates. 9. Photo-oxidation of proteins causes the formation of aggregates, indicating denaturation. 10. Hematoporphyrin migrates with the albumin fraction of unaltered as well as the photo-oxidized anti-egg albumin rabbit serum and pneumococcus Type I horse serum; in isolated proteins such as egg albumin, globulin gamma, or Felton solution, etc., the dye moves independently of the protein; after progressive photo-oxidation Hp becomes progressively fixed to the protein. Eosin behaves similarly to hematoporphyrin.

show abstract

Electrophoresis of serum globulin

Cited by 303 publications

References 7 publications

Electrophoretic Analysis of the Proteins of Plasma and Serous Effusions

Electrophoretic Analysis of the Proteins of Plasma and Serous Effusions

Electrophoretic Analysis of Plasma and Urinary Proteins

Studies on Photo-Oxidation of Antigen and Antibodies

Contact Info

Product

Resources

About