Variations among gamma-globulins at the antigenic site revealed by pepsin digestion.

Williams, Ralph C.; Lawrence, Thomas G.

doi:10.1172/jci105386

Cited by 20 publications

(12 citation statements)

References 19 publications

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“…Furthermore, polysaccharides are heat-resistant, very heterogeneous and could influ ence protein conformation [7]. Similar IgM and IgG Ab to those observed by us, though reacting only with the F(ab' )2 fragments of IgG and IgA, have been dem onstrated and are known as pepsin agglutinators [20,28,29].…”

Section: Discussionsupporting

confidence: 63%

“…Moreover, since the papain Fci; fragment and the isolated e(DES) heavy chains as well as aggregates of IgE(DES) prepared by reduction alkylation were unreactive, this might indicate that the epitope is located in the hinge region, being con formational and necessitating the interaction between intact light and heavy chains for its expression. Simi lar epitopes have been described for immunoglobu lins of other isotypes [20,21] and the disulphide bridges in the Ct-2 domain are known to be important for the conformation of IgE [6]. The reactive papain 6S,--fragment is in keeping with that this fragment re presents IgE(DES) which has lost one of its two Fab fragments [Magnusson, unpublished data].…”

Section: Discussionmentioning

confidence: 99%

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Autoantibodies of the IgM Class against a Human Myeloma Protein IgE(DES). II. Specificity

Magnusson

Vaerman

1986

Int Arch Allergy Immunol

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Five different monoclonal IgE proteins, papain and pepsin fragments of myeloma protein IgE(DES) and particle-counting immunoassay were used to study in detail the epitope(s) of IgE(DES) involved in the agglutination with IgM anti-IgE(DES) antibodies. The specificity of these autoantibodies was restricted to IgE(DES) as they did not react with latex particles coated with four other IgE myeloma proteins. Antibodies reactive with latex-IgE other than latex-IgE(DES), when present, were also of restricted specificity as shown by criss-cross absorption experiments. These differences between IgE myeloma proteins could not be attributed to the light chain type nor to the Em(l)-allotype. The epitope(s) of IgE(DES) participating in the reaction was heat-resistant (56 °C, 2 h) and localized in the pepsin F(ab′)_2ε fragment, but was absent in the papain Fc_ε and Fab_ε fragments. Further degradation by pepsin of the F(ab′)_2ε fragment (molecular weight 145,000 daltons) to 5S_ε (90,000 daltons) and Fc_εXXX fragments (30,000 daltons) destroyed the reacting epitope. These results indicate that the IgM antibodies were not directed against k chain or idiotypic determinants of IgE(DES), but to some epitope(s) in the undegraded hinge region. Therefore, it seems that some kind of antigenic heterogeneity, perhaps related to the carbohydrate moieties, is present in IgE myeloma proteins besides the known idiotypic, allotypic and isotypic ones.

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Section: Discussionsupporting

confidence: 63%

Section: Discussionmentioning

confidence: 99%

Autoantibodies of the IgM Class against a Human Myeloma Protein IgE(DES). II. Specificity

Magnusson

Vaerman

1986

Int Arch Allergy Immunol

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“…Pepsin digestion of autologous individual 5,-globulins isolated by zone electrophoresis produced inhibition to log~ dilution of 12. On the basis of this and previous work utilizing pepsin-digested myeloma proteins (7), it was possible to estimate that concentrations of 0.03-0.015 mg/cc of material bearing antigenic determinants similar to those exposed by pepsin digestion of ~,G were present in the fractions from DEAE-cellulose columns tested. In addition, initial peaks obtained from three normal sera by DEAE-ceUulose columns at pH 8.0, 0.02 ~ phosphate were tested for inhibitory capacity.…”

Section: Resultsmentioning

confidence: 99%

“…Fractions were tested in immune diffusion against rabbit antisera specific for human Fc fragment, F(ab')2, and against anti-F(ab')2 antiserum absorbed with pooled L chains from Cohn fraction II. (7)…”

Section: Methodsmentioning

confidence: 99%

STUDIES OF HUMAN ANTI-γ-GLOBULIN FACTORS REACTING WITH PEPSIN-DIGESTED Γ-Globulins

Lawrence¹,

Williams²

1967

The Journal of Experimental Medicine

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Many sera from normal individuals as well as patients with various disease states contain agglutinating antibodies which show specificity for antigenic determinants of γ-globulin revealed by pepsin digestion at pH 4.1. Sera containing such agglutinating activity as well as sera negative for these agglutinators contain low molecular weight (3S–5S) components of slow γ-mobility which inhibit these agglutination reactions. Low molecular weight inhibitors show both auto- and isospecificity, and are antigenically related to the 5S pepsin fragment of γ-globulin. A common situation is thereby revealed in which human anti-γ-globulin antibodies showing specificity for pepsin-digested γ-globulins are present in serum along with low molecular weight γ-globulin components capable of inhibition. Autoreactivity or autospecificity of such anti-γ-globulin factors is a phenomenon shared by both normal human sera and sera from patients with various disease states.

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“…Antisera against IgA were rendered specific by absorption with serum deficient in IgA. An antiserum capable of differentiating IgAl-and IgA2-proteins (13)(14)(15) (16). The digestion reactions were halted at the desired time either by dialysis against phosphatebuffered saline pH 7.4 or by application of the digestion mixture to a Sephadex G200 column equilibrated with phosphate-buffered saline pH 7.4.…”

Section: Methodsmentioning

confidence: 99%

Two distinct groups of immunoglobulin A(IgA) revealed by peptic digestion

Wilson¹,

Williams²

1969

J. Clin. Invest.

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Variations among gamma-globulins at the antigenic site revealed by pepsin digestion.

Cited by 20 publications

References 19 publications

Autoantibodies of the IgM Class against a Human Myeloma Protein IgE(DES). II. Specificity

Autoantibodies of the IgM Class against a Human Myeloma Protein IgE(DES). II. Specificity

STUDIES OF HUMAN ANTI-γ-GLOBULIN FACTORS REACTING WITH PEPSIN-DIGESTED Γ-Globulins

Two distinct groups of immunoglobulin A(IgA) revealed by peptic digestion

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