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

Hellsing, Krister

doi:10.1042/bj1140145

Cited by 27 publications

(7 citation statements)

References 10 publications

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“…Immunodiffusion was performed in a 1% agar gel containing 40 mg of Dextran 10/ml (Hellsing, 1969) poured on microscope slides with L.K.B. Immunophor equipment.…”

Section: Methodsmentioning

confidence: 99%

Electrophoretic and immunological charactorization of rat neurophysin

Norström

Sjöstrand

Livett

et al. 1971

Biochemical Journal

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1. The electrophoretic properties of rat posterior pituitary proteins have been compared on starch gel with those of bovine and porcine neurophysins. 2. [(35)S]-Cysteine was injected into the supraoptic nucleus of male rats and 16-24h later the distribution of labelled neural-lobe protein in starch and polyacrylamide gels was determined. In both systems a single major protein component was found to contain more than 80% of the total recovered radioactivity. Between 5 and 10% of the radioactivity was found in a minor component in polyacrylamide gel. 3. In agar, microimmuno-diffusion and -electrophoresis of the rat neural-lobe proteins gave a single arc with neurophysin antiserum, and after starch-gel electrophoresis this arc was shown to be due to the major labelled component. 4. The molecular weights of the rat neural-lobe proteins were estimated by polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate. The molecular weight of the major labelled component was found to be 12000. 5. It is concluded that the rat neurophysin consists of one major and possibly one minor component.

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“…Immunodiffusion was performed in a 1% agar gel containing 40 mg of Dextran 10/ml (Hellsing, 1969) poured on microscope slides with L.K.B. Immunophor equipment.…”

Section: Methodsmentioning

confidence: 99%

Electrophoretic and immunological charactorization of rat neurophysin

Norström

Sjöstrand

Livett

et al. 1971

Biochemical Journal

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“…Commercial preparations of serum albumin usually contain dimers and higher oligomers (Pedersen, 1962;Andersson, 1966;Hellsing, 1969;Janatova, 1974;Blaabjerg & Hyltoft Petersen, 1979). The concentrate purchased for these experiments appeared to contain approx.…”

Section: A Lbumin Preparationsmentioning

confidence: 99%

The exclusion of human serum albumin by human dermal collagenous fibres and within human dermis.

Bert¹,

Mathieson²,

Pearce³

1982

Biochemical Journal

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Preparations of dermal collagenous fibres and slices of human dermis have been equilibrated with 125I-labelled monomeric human serum albumin. The space inaccessible to the albumin in the fibres and in the dermis was determined by subtraction of the accessible space, calculated from the radioactivity of the specimen, from its total fluid. For a fibre preparation examined in detail, the fluid exclusion was independent of the concentration of either albumin or collagen. Binding of albumin to the fibres was not demonstrable. Three fibre preparations excluded albumin from 3.75 +/- 0.96, 3.55 +/- 0.67, and 2.05 +/- 0.39 g of fluid/g of collagen (+/-S.D.). Slices from three specimens of dermis excluded albumin from 1.45 +/- 0.08 g of fluid/g of insoluble solids or 1.57 +/- 0.11 g of fluid/g of collagen (+/-S.D.). Thus the exclusion of albumin by dermis was much less than expected from its content of collagenous fibres. On the basis of these data and the published composition of dermis, the concentration of albumin in the accessible interstitial space was estimated to be close to that in the plasma.

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“…Polymer enhancement also produces a shift in the equivalence zone to higher antigen concentrations (13) by reducing the solubility of smaller antigen-antibody complexes formed in the region of excess antigen. The sensitivity of the reaction is enhanced by the increase in the mean size of the aggregates in the presence of polymers (9). These changes in the reaction permit the use of less potent antisera or smaller volumes ofhigh-titer antisera to achieve the desired reaction intensity.…”

Section: Discussionmentioning

confidence: 99%

“…These assays have been criticized for being difficult to standardize and reproduce, inaccurate, and too expensive for rou-tine use because of high antiserum consumption (7,16). These difficulties were overcome when Hellsing (9) reported the enhancement of antigen-antibody aggregation by the inclusion of polyethylene glycol 6000 (PEG) in the reaction medium.…”

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confidence: 99%

Improved streptococcal grouping antisera containing polyethylene glycol

George¹,

Ashworth²,

Facklam³

et al. 1981

J Clin Microbiol

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Antisera to streptococcal groups A through G containing 4% polyethylene glycol 6000 were prepared and evaluated. Seventy strains of homologous and heterologous beta- and non-beta-hemolytic streptococci were included in the evaluation. Homologous reactions were determined against extracts prepared by four extraction methods: hot hydrochloric acid (Lancefield) extraction, autoclave extraction, hot formamide extraction, and nitrous acid extraction. Enhancement of the precipitin reaction in the presence of polyethylene glycol 6000 permitted a fourfold dilution of all antisera for use in the capillary precipitin test. At this dilution, the potency of the antisera exceeded requirements established for these reagents.

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

Cited by 27 publications

References 10 publications

Electrophoretic and immunological charactorization of rat neurophysin

Electrophoretic and immunological charactorization of rat neurophysin

The exclusion of human serum albumin by human dermal collagenous fibres and within human dermis.

Improved streptococcal grouping antisera containing polyethylene glycol

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