Electrophoretic Analysis of the Proteins of Plasma and Serous Effusions

Abstract

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

The Electrophoretic Distribution of Proteins in Plasma in Rheumatoid Arthritis12

“…The extreme variation from high concentrations of al-and a2-globulins, associated with normal .y-globuilin (Figure lb) to marked elevation of the y-fraction in the presence of only a slight abnormality of the a-globulins (Figure lc) Table IV.) These findings are similar to those described by Olhagen (4, 10) and Dole and Rothbard (9) in rheumatoid arthritis and those noted in the course of other diseases (35)(36)(37).…”

The Effects of Induced Malaria, Acute Starvation and Semi-Starvation on the Electrophoretic Diagram of the Serum Proteins of Normal Young Men 1

“…The changes noted during malaria here are similar to those seen in pneumonia (19), scarlet fever (16), rheumatic fever (16), and tonsillitis (20). In contrast, no such changes were seen in acute starvation in spite of the fact that the subjects in the latter experiments lost roughly 50 grams of nitrogen each.…”

Experiences With Renal Homotransplantation in the Human: Report of Nine Cases 1

“…to depressed formation of serum protein in nephritis (13). In the nephrotic syndrome the hypoproteinemia is characterized by very low levels of gamma globulin, in spite of the reversed A/G ratio (85,86,125). There is some evidence that under these circumstances antibody formation and resistance to infection is decreased (16,17,42,67,87,91), although this has been disputed by others (6,8,100).…”