Quantitative Studies on the Precipitin Reaction

Heidelberger, Michael; Kendall, Forrest E.; Teorell, Torsten

doi:10.1084/jem.63.6.819

Cited by 48 publications

(19 citation statements)

References 5 publications

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“…This behavior is analogous, in part, to that observed by Heidelberger, Kendall, and Teorell (36), for the influence of high concentrations of NaCI on the reaction of SIII with the homologous antibody, although there, in contrast to the present data, the general course of the reaction was not altered. In neither instance was the effect of salts directed toward an increased solubility of the precipitate since no additional precipitation occurred upon dialysis unless more antigen was added.…”

Section: 4-supporting

confidence: 89%

“…have suggested that competition of the cation with the antibody for combination with the acidic groups of the polysaccharide is responsible for the inhibitory effect of concentrated NaC1 (36). Undoubtedly this does not apply to the present phenomenon since it is an anionic effect, and hence it can hardly be explained in terms of an electrostatic shielding of these groups.…”

Section: 4-mentioning

confidence: 70%

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Immunochemical Properties of Native and Denatured Horse Serum Globulins

Erickson

Neurath

1945

Journal of General Physiology

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The problem of the relation of antibodies to normal serum globulins has been approached in the past by comparison of their chemical, physical, and immunological properties in the native state (cf. 1-3). Little information is available, however, on their relative behavior in the denatured state. This paper describes an investigation of the effects of denaturation by guanidine hydrochloride on certain physicochemical and immunological properties of Type I antipneumococcal horse serum globulin. In the fight of recent theories of the structure and synthesis of antibodies (4, 5) it appeared also of interest to determine whether denaturation of normal and immune globulin might accentuate or diminish the antigenic relations which exist between them in the native form.Comparative physicochemical properties of normal and immune serum globulins have been reviewed by Kabat (3). Wright (6) has reported that the antigenic nature of horse antibody proteins is essentially the same as that of horse normal gamma globulin. However, quantitative investigations by Treffers et al. (7)(8)(9) based on earlier findings of Ando et al. (10), and Marrack and Duff (11), revealed that antipneumococeal horse serum globulin differs from normal gamma globulin in its reaction with an antispecific precipitate rabbit serum. A high degree of cross-reactivity existed, and it was further noted that those antibodies that were precipitated by either antigen were incapable of differentiating between the two. These investigations provided experimental proof for earlier suggestions (12) that the groups on the antibody molecule responsible for antibody activity are unrelated to those involved in antigenic specificity.Previous work on the effects of denaturation on the serological and physicochemical behavior of immune globulins has been extensively reviewed (1,13,14). The observation that monolayers of Types i and III antipneumococcal rabbit globulin are serologic.ally active (15), suggests the independence of serological activity of a unique stereochemical configuration. However, in the light of a recent hypothesis (16) that formation of protein films involves the separation of preformed layers of peptide chains rather than unfolding into individual chains, a functional relation between intact two dimensional configurations and antibody activity is not excluded.

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Section: 4-supporting

confidence: 89%

Section: 4-mentioning

confidence: 70%

Immunochemical Properties of Native and Denatured Horse Serum Globulins

Erickson

Neurath

1945

Journal of General Physiology

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“…of the mixture per injection as above. If not immediately used, the antisera obtained from these rabbits were frozen and stored at -18 0 C. The titer of the antisera was obtained by measuring the total protein content of the precipitate, 48 or by a radioisotopic technic, 49 using I-125 labeled guinea pig y, | S and a globulins. 50 For the insulin antibody assay radioactive insulin was diluted with a 1 per cent bovine serum albumin in borate buffer (^H 8.5, 0.13M) and with carrier crystalline beef insulin; the final concentration of insulin-I-125 w a s 3-8 uc.…”

Section: Methodsmentioning

confidence: 99%

Studies on Experimental Insulin Immunity: I. Dynamics of Insulin Immunity in the Guinea Pig

Horino

Blumenthal

1966

Diabetes

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Insulin half life and the formation and characterization of the insulin-binding antibodies have been studied in the guinea pig both in vivo and in vitro. The antigen-antibody complexes have also been studied utilizing cellulose column electrophoresis and Sephadex G-200 column filtration. In addition, a quantitative assay procedure for insulin-binding antibodies has been employed. In normal guinea pigs the injected insulin-I-125 is carried by at least two serum proteins, presumably albumin and an α. globulin, or more specifically 4.5S and 19S proteins. In immune animals the insulin-antibody complexes are represented by a single peak in the (β-γ globulin region on column electrophoresis; they are distinguishable from the uncomplexed antibodies which are 7S γ1 and 7S γ1 globulins. The precipitating insulin antibody also appears to be a 7S globulin. Moreover, the insulin-antibody complexes occur as a single component in the 19S fraction on Sephadex G-200 filtration, and if the complex were a single molecule it would have a molecular weight equivalent of about 630,000. During the immunization process the insulin binding antibody titer increases progressively in association with an elevation of 7S globulin. In most animals during the early stages of immunization the molecular weight of the antibodies appears to be exclusively of the 7S globulin type; however, in two of seven animals there was, in addition, a small amount of insulin antibody of 19S globulin type early during the immunization period. The purpose in estimating a molecular weight equivalent of the insulin-antibody complex relates to the possibility that the distinctive features of the angiopathies of diabetes may depend upon certain physicochemical characteristics of this complex.

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“…A study by Heidelberg et al [22] noted that increasing NaCl concentration above 0.15 M would reduce the complexing of antibody with antigen. The gel filtration procedure was therefore repeated, but the proteins were eluted from the column with 0.7 M NaCl in 0.001 M phosphate buffer, pH 7.…”

Section: Fraction Numbermentioning

confidence: 99%

The Antigens of Pigeon Breeder’s Disease

Krause-Hooyman

Fredricks

1983

Int Arch Allergy Immunol

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Two esterase activities were detected in pigeon dropping extracts (PDE). The first exhibited the ability to cleave p-tosyl-L-arginine methyl ester (TAMe), and the second utilized α-naphthyl acetate as its substrate. Both enzymes were stable at a temperature of 60°C. Although the enzymes could be separated from each other through gel filtration chromatography, both were associated with PDE₁ (a major antigen found in pigeon droppings) throughout the fractionation procedure. In addition, it was shown that the TAMe esterase exhibited protease activity by virtue of its ability to hydrolyze α-casein.

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Quantitative Studies on the Precipitin Reaction

Cited by 48 publications

References 5 publications

Immunochemical Properties of Native and Denatured Horse Serum Globulins

Immunochemical Properties of Native and Denatured Horse Serum Globulins

Studies on Experimental Insulin Immunity: I. Dynamics of Insulin Immunity in the Guinea Pig

The Antigens of Pigeon Breeder’s Disease

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