Double Diffusion System Research Articles

Elektronenoptische Untersuchungen über die Feinstruktur des visceralen Dottersackepithels der Ratte nach intrauteriner Injektion eines Kaninchen-Antirattenplacentaserums oder eines Kaninchen-Normalserums

Elektronenoptische Untersuchungen über die Feinstruktur des visceralen Dottersackepithels der Ratte nach intrauteriner Injektion eines Kaninchen-Antirattenplacentaserums oder eines Kaninchen-Normalserums

Bovine 37S iodoprotein: Isolation and characterization

A thyroglobulin-like protein with a sedimentation constant of 36.6S has been isolated from bovine thyroid glands and further characterized. Its molecular weight, 2 × 10 6, is close to three times that of 19S thyroglobulin, the major thyroid iodoprotein. The amino acid composition of this iodoprotein also closely resembled that of 19S thyroglobulin and of the 27S iodoprotein. A reaction of identity in a double diffusion system with 19S, 27S and 36.6S has also been found. The iodine content of the 36.6S iodoprotein was greater than that of 19S thyroglobulin, but similar to that of the 27S species isolated from the same thyroid extract.

A general method of increasing the sensitivity of immune diffusion its application to CEA

A method is described for increasing the sensitivity of methods employing immune diffusion. In theory the increase is limited only by the patience of the experimenter; in practice increases of 5-fold are routinely obtainable, and the method holds the potential for greater gains in sensitivity because it can be combined with the use of “intensifiers” such as polyethylene glycol (PEG), tannin and fluorescent antibodies. Its application is illustrated for CEA (carcinoembryonic antigen) in the double diffusion system of Ouchterlony, in radial immunodiffusion, in simple electrophoresis, in immunoelectrophoresis, in counter-immunoelectrophoresis and in Laurell's method of electrophoresis of proteins into antibody-containing gel.

The Dissociation of Human Serum 7S and Bovine Colostrum Immune Globulins into Subunits by Reduction-Alkylation-Succinylation

Abstract Human 7S and bovine colostral immunoglobulins were succinylated and reduced-alkylated, and their subunits were separated by chromatography on Sephadex G-200 columns. Human 7S immunoglobulin yielded heavy chains with a molecular weight of 55,700 and light chains with a molecular weight of 22,300. Bovine colostral immunoglobulins gave heavy and light chains with molecular weights of 49,500 and 25,200, respectively. Since the molecular weight of the colostral immunoglobulin of 166,000 is not accounted for by two heavy and two light chains, the possibility is raised that another subunit possibly exists in colostral immunoglobulin. The succinylated proteins lost their ability to form precipitin lines with antisera to native bovine and human immunoglobulins, but they formed precipitin lines in the double diffusion system with an antiserum to the succinyl hapten residues.

Immunological studies of liver, kidney, and muscle fructose 1,6-diphosphatases

Immunological methods were employed to investigate possible structural relations between fructose 1,6-diphosphatases present in rabbit liver, kidney, and muscle. The liver and kidney enzymes were found to be immunologically identical, and distinct from the muscle enzyme. Liver and kidney fructose 1,6-diphosphatases were each inhibited approximately 80% by antiserum prepared against pure liver FDPase, whereas the activity of the muscle enzyme was not affected. In the Ouchterlony double-diffusion system liver and kidney FDPases gave a single continuous precipitin band of identity, and also behaved identically in immunoelectrophoresis. Muscle FDPase gave no precipitin bands in these tests and by activity stain was shown to have a different electrophoretic mobility. A method for the purification of rabbit kidney FDPase is described which yields a homogeneous preparation in high yield.

Further purification and characterization of a placental protein with immunological similarity to human growth hormone.

Josimovich and MacLaren1 purified a substance from human placentas which cross-reacted immunologically with antiserum to human growth hormone in Ouchter-lony's double-diffusion system. Moreover, they detected this substance in the blood and urine of pregnant women, thereby raising the possibility that it might be a new placental hormone. Investigation of the physiological role of this substance has been hampered by the limited supply of material. The relatively easy method outlined here yields substantially greater quantities of this substance than could be obtained by the previously described purification from fresh-frozen placentas2.

The altered pattern of diffusion in a double-diffusion system I. Between two sources of one reactant

The altered diffusion pattern in a double-diffusion system results from the altered properties of the medium. Assuming, in accordance with the available evidence, that the diffusion of reactant depends on the ratio of concentration gradients of the reactant and dissolved substances in the gel which diffuse against the reactant, an increase of this ratio in the area between two diffusing sources results in an altered rate of diffusion.The diffusion experiments with and without chemical reaction revealed that the mechanism of the alteration of the diffusion rate in the system is independent of the presence of reagent in the gel.