Separation of Univalent Fragments of Rabbit Antibody by Reduction of a Single, Labile Disulphide Bond

Nisonoff, Alfred; Markus, Gabor; Wissler, F.C.

doi:10.1038/189293a0

Cited by 131 publications

(42 citation statements)

References 9 publications

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“…This model provides a basis for explaining the cleavage of y-globulin by papain and cysteine into fragments of different antigenic structure and biological activity (7,(14)(15)(16). Certain peptide bonds (17) of H chains may be hydrolyzed more rapidly by papain than any of the peptide bonds of L chains, thus releasing large fragments of different properties, particularly after cleavage of a labile disulfide bond holding the S fragments together (18).…”

Section: Discussionmentioning

confidence: 99%

The ANTIGENIC STRUCTURE OF THE POLYPEPTIDE CHAINS OF HUMAN Γ-Globulin

Olins

Edelman

1962

The Journal of Experimental Medicine

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One of the goals of chemical and immunological studies of T-globulins is to relate the biological activities of the whole molecules to structural features of their constituent polypeptide chains. 7S ~'-globulin molecules consist of multiple polypeptide chains linked by disulfide bonds and non-covalent interactions (1). Two types of chains have been described (2, 3): light (L) chains, having molecular weights of approximately 20,000; and heavy (H) chains, having molecular weights greater than 50,000. Certain physicochemical characterisitics of L chains have been associated with differences in the specificity of antibodies (4), with the individuality of myeloma proteins (5), and with the unique thermosolubility properties of Bence-Jones proteins (3). The current evidence and hypotheses relating the properties of normal and pathological "y-globulins to properties of their L and H chains have been reviewed (6).The present study is concerned with an analysis of the antigenic characteristics of the polypeptide chains of normal human 7S %globulin and of a human myeloma protein. The antigenic determinants of L and H chains have been correlated with the previously described S and F determinants (7), which comprise two major non-cross-reacting antigenic groups of the whole "},-globulin molecule. Antigenic identity has been found between the L chains of a myeloma protein and the Bence-Jones protein from the same patient, thus providing further evidence of their structural similarity, and corroborating the results of previous chemical studies (3).These results furnish a basis for relating the polypeptide chains of qt-globulin molecules to the fragments produced by hydrolysis with papain. Methods and Materials'y-Globul~ns.--Lyophillzed human 7S T-globulln was obtained as fraction II of Cohn (Lot C-679) from Lederle Laboratories (Pearl River, New York). A portion was further purified by zone electrophoresis on starch (8). The preparation of a "y-myeloma protein (patient Haw) and Bence-Jones protein from the same patient has been described previously (3). Protein concentrations were determined by measurement of the optical density of solutions at 280 m# and by a modification of the Folin-Ciocalteu method (9).

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Section: Discussionmentioning

confidence: 99%

The ANTIGENIC STRUCTURE OF THE POLYPEPTIDE CHAINS OF HUMAN Γ-Globulin

Olins

Edelman

1962

The Journal of Experimental Medicine

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“…The anti-Id antibodies eluted from both columns did not bind to any of the Igs used to coat the control dishes. To rule out the possibility that the binding of the anti-Id antibody to the antifibrinogen antibody-coated EIA plates was due to interaction through its Fc portion, BLAhL a~~~~~- F(ab')2 fragments of the anti-Id antibody were prepared as described (31) and tested in the EIA system against both autologous and rabbit antifibrinogen antibodies. The binding of F(ab')2 fragments was not different from that of the whole antibody molecule.…”

Section: Resultsmentioning

confidence: 99%

Spontaneous reversal of acquired autoimmune dysfibrinogenemia probably due to an antiidiotypic antibody directed to an interspecies cross-reactive idiotype expressed on antifibrinogen antibodies.

Ruı́z-Argüelles¹

1988

J. Clin. Invest.

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A young man with a long history of abnormal bleeding was seen in January 1985. Coagulation tests showed dysfibrinogenemia and an antifibrinogen autoantibody was demonstrable in his serum. This antibody, when purified, was capable of inhibiting the polymerization of normal fibrin monomers, apparently through binding to the a fibrinogen chain. 6 mo later the patient was asymptomatic, coagulation tests were normal, and the antifibrinogen autoantibody was barely detectable. At this time, affinity-purified autologous and rabbit antifibrinogen antibodies were capable of absorbing an IgG kappa antibody from the patient's serum, which reacted indistinctly with both autologous and xenogeneic antifibrinogen antibodies in enzyme immunoassays. It has been concluded that the patient's dysfibrinogenemia was the result of an antifibrinogen autoantibody, and that later on an antiidiotype antibody, which binds an interspecies cross-reactive idiotype expressed on anti-human fibrinogen antibodies, inhibited the production of the antifibrinogen autoantibody which led to the remission of the disorder.

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“…(F(ab')z : pepsin-treated antibody, a dimer of two identical units, the Fab' fragments, each with one combining site, linked by one disulfide bond [3,4] ). The complex proved to be useful for measuring human IgG as little as 0.3 fmol(50 pg) by sandwich method.…”

Section: Methodsmentioning

confidence: 99%