Immune reactions in polysaccharide media. Polysaccharide-enhanced precipitin reactions with antigens of various sizes

The influence of the size of the antigen in the polysaccharide-enhanced precipitin reaction was investigated. The experiments were carried out by addition of homologous antigens of different molecular sizes (the monomer, dimer and trimer of serum albumin and the monomer and dimer of immunoglobulin G) to the same preparation of antibody in the absence and presence of dextran. Dextran decreased the solubility of the immune complexes to a larger extent when the antigen size increased. This is in accord with the view that the polysaccharide effect is due to steric exclusion.

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Immune reactions in polysaccharide media. The composition of the antigen–antibody complexes in the precipitin reaction

Biochemical Journal ◽

10.1042/bj1140141 ◽

1969 ◽

Vol 114 (1) ◽

pp. 141-144 ◽

Cited By ~ 13

Author(s):

Krister Hellsing

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Immunoglobulin G ◽

Immune Complexes ◽

Aggregate Size ◽

Precipitin Reaction ◽

Soluble Immune Complexes ◽

Immune Aggregates ◽

Antigen Antibody ◽

Free Antigen

The precipitin reaction is enhanced in the presence of polysaccharides (Hellsing, 1966). This reaction has now been studied in detail with labelled antigen (125I-labelled human serum albumin) and antibody (131I-labelled rabbit anti-albumin immunoglobulin G). The relative proportions of antigen and antibody in the precipitates are unchanged by the addition of dextran in spite of the increased precipitation. The ratio of antibody to antigen in the soluble immune complexes decreases with increasing polysaccharide concentration. This can be interpreted as a decrease in the aggregate size of the complexes. At the same time the amount of free antigen in the solution increases. The results are consistent with a decrease in solubility, primarily of the large immune aggregates, together with a shift in the equilibrium between small and large complexes. The effect is in accord with a steric-exclusion phenomenon.

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Immune reactions in polysaccharide media. Investigation on complex-formation between some polysaccharides, albumin and immunoglobulin G

Biochemical Journal ◽

10.1042/bj1120483 ◽

1969 ◽

Vol 112 (4) ◽

pp. 483-487 ◽

Cited By ~ 18

Author(s):

Krister Hellsing

Keyword(s):

Sodium Chloride ◽

Complex Formation ◽

Serum Albumin ◽

Immunoglobulin G ◽

Phosphate Buffer ◽

Equilibrium Dialysis ◽

Immune Reactions ◽

Precipitin Reaction ◽

Specific Complex

Serum albumin and immunoglobulin G were chromatographed on columns of dextran, hyaluronate and chondroitin 4-sulphate. The partition of the two proteins between hyaluronate and buffer was also measured by equilibrium dialysis. The results accord with the view that there is no complex-formation between the polysaccharides and the proteins in 0·05m-phosphate buffer, pH7·4, containing sodium chloride (0·1m). The observations support the hypothesis that the previously described polysaccharide enhancement of the precipitin reaction is due to exclusion and not to non-specific complex-formation.

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Immune reactions in polysaccharide media. Experiments with specific antibodies of different affinities for serum albumin

Biochemical Journal ◽

10.1042/bj1140151 ◽

1969 ◽

Vol 114 (1) ◽

pp. 151-155 ◽

Cited By ~ 18

Author(s):

Krister Hellsing

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Rabbit Antibody ◽

Immune Reactions ◽

Specific Antibodies ◽

Precipitin Reaction ◽

Immune Precipitation ◽

Exclusion Mechanism ◽

Immunological Assays

Rabbit antibody fractions of different affinities for human serum albumin were prepared by an immunosorbent technique. The fractions were used in studies on the enhancement of the precipitin reaction by polymers. Dextran increased the immune precipitation to about the same extent regardless of whether antibodies with high and low affinities were used. The effect should considerably facilitate the detection of antibodies with low precipitating ability in immunological assays. The results are discussed in terms of a steric-exclusion mechanism.

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Immunohistochemical detection of Fc receptor. I. Light microscopic demonstration of Fc receptor by using soluble immune complexes of peroxidase-antiperoxidase immunoglobulin G.

Journal of Histochemistry & Cytochemistry ◽

10.1177/25.4.404351 ◽

1977 ◽

Vol 25 (4) ◽

pp. 252-258 ◽

Cited By ~ 11

Author(s):

G Itoh ◽

S Miura ◽

I Suzuki

Keyword(s):

Cell Surface ◽

Immunoglobulin G ◽

Immune Complexes ◽

Surface Characterization ◽

Fc Receptor ◽

Frozen Sections ◽

Microscopic Demonstration ◽

Lymph Node Cells ◽

Soluble Immune Complexes ◽

And Control

The mouse mesenteric lymph node cells (in the cell suspension and frozen sections) were incubated in the soluble immune complexes of peroxidase-antiperoxidase immunoglobulin G. After being washed, they were reacted with diaminobenzidine tetrahydrochloride. Light microscopically brown-colored granules were observed on the cell surface of a proportion of small lymphocytes. In frozen sections, a proportion of small lymphocytes were stained dark brown on the cell surface. Characterization and control experiments suggest that the binding of peroxidase-antiperoxidase immunoglobulin G to the cell surface is mediated by Fc receptor. Peroxidase-antiperoxidase immunoglobulin G, therefore, can be used as in indicator of Fc receptor.

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Cooking Temperature of Turkey Ham Affects Lactate Dehydrogenase, Serum Albumin and Immunoglobulin G as Determined by ELISA

Journal of Food Science ◽

10.1111/j.1365-2621.1996.tb14761.x ◽

1996 ◽

Vol 61 (1) ◽

pp. 209-212 ◽

Cited By ~ 10

Author(s):

D.M. SMITH ◽

L.D. DESROCHER ◽

A.M. BOOREN ◽

C.H. WANG ◽

M.M. ABOUZIED ◽

...

Keyword(s):

Lactate Dehydrogenase ◽

Serum Albumin ◽

Immunoglobulin G ◽

Cooking Temperature

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Immune reactions in polysaccharide media. The effect of hyaluronate, chondroitin sulphate and chondroitin sulphate–protein complex on the precipitin reaction

Biochemical Journal ◽

10.1042/bj1120475 ◽

1969 ◽

Vol 112 (4) ◽

pp. 475-481 ◽

Cited By ~ 24

Author(s):

Krister Hellsing

Keyword(s):

Molecular Weight ◽

Human Serum Albumin ◽

Connective Tissue ◽

Immune Complexes ◽

Protein Complex ◽

Chondroitin Sulphate ◽

Pathological Conditions ◽

Precipitin Reaction ◽

Soluble Immune Complexes ◽

Antigen Antibody

The influence of the connective-tissue polysaccharides hyaluronate, chondroitin 4-sulphate and a chondroitin 4-sulphate–protein complex (PP-L) from cartilage on the precipitin reaction was investigated. In a system consisting of 125I-labelled human serum albumin and the immunoglobulin G fraction from rabbit anti-albumin sera, the precipitation is greatly increased in the region of antigen excess. This effect depends on the concentration, molecular weight and configuration of the polysaccharide. The increase parallels a decrease in the amount of soluble immune complexes in the supernatant. It is suggested that the effect is due to steric exclusion of the complexes from the domains of the polysaccharides. The possibility that such a mechanism might enhance precipitation of antigen–antibody complexes in certain pathological conditions is discussed.

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