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

Olins, Donald E.; Edelman, Gerald M.

doi:10.1084/jem.116.5.635

Cited by 79 publications

(35 citation statements)

References 20 publications

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“…The bands had mobilities identical with those of several of the L chain bands of the reduced alkylated antibodies from which the S fragment was derived. This evidence, considered along with previous immunologic findings (12), suggests that L chains are present complete or almost complete in the S fragment. In these experiments there was no starch gel electrophoretic evidence of the H chain fragment postulated (3) to be present in the S fragment in addition to the L chain.…”

Section: Discussionmentioning

confidence: 84%

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Structure and Specificity of Guinea Pig 7s Antibodies

Edelman

Benacerraf

Óváry

1963

The Journal of Experimental Medicine

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In an earlier study (1), reproducible differences in structure were found among antibodies of different specificities from individual guinea pigs. The structural variations were revealed by dissociating the antibodies into their L and H polypeptide chains (2, 3). Starch gel electrophoresis of different dissociated antibodies revealed differences in the number and mobility of the multiple sharp bands corresponding to L chains. In striking contrast, the patterns of dissociated non-specific 3,-globulins from the same animals showed diffuse zones in the L chain region.The present experiments were designed to extend these observations and to answer several questions that arose in the course of the work. One set of questions concerns the effect of different procedures of immunization, the role of the carrier protein to which the haptens are conjugated, and the influence upon the electrophoretic patterns of fine differences in the immunologic specificity of the antibodies. The other group of questions bears upon the origin of the multiplicity of the L chain bands of antibodies directed against a single hapten and also upon the location of L chains in the antibody molecule.

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Section: Discussionmentioning

confidence: 84%

“…Several investigations (3,(12)(13)(14) have demonstrated that the antigenic determinants of L chains are on the S fragment. This fragment, which contains the antibody combining site (10, 15) yielded distinct bands after reduction and alkylation and starch gel electrophoresis.…”

Section: Discussionmentioning

confidence: 99%

Structure and Specificity of Guinea Pig 7s Antibodies

Edelman

Benacerraf

Óváry

1963

The Journal of Experimental Medicine

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“…Antigenic differences between Bence Jones protein and the S fragment of autologous myeloma protein have been demonstrated (18). By double diffusion methods, the L chain of myeloma protein does show a reaction of partial identity with the S fragment of the same protein; however, the L chain more closely resembles the autologous Bence Jones protein than does the S fragment (19). Indeed, Edelman and Gally (1) and showed similar amino acid compositions.…”

Section: Discussionmentioning

confidence: 99%

“…Studies relating Bence Jones protein to the serum myeloma protein have been in terms of the S or slow fragment obtained by papain treatment (11)(12)(13)(14)(15) and the L polypeptide chain obtained by reduction and alkylation of the purified serum protein (1,16,17). Antigenic differences between Bence Jones protein and the S fragment of autologous myeloma protein have been demonstrated (18).…”

Section: Discussionmentioning

confidence: 99%

Macroglobulinemia with Bence Jones Proteinuria: Comparison of Urinary Protein and L Chain of Serum Proteins*

Gross¹,

Epstein²

1964

J. Clin. Invest.

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Edelman and Gally (1) have recently shown that an individual's Bence Jones proteins are chemically and physically similar to the low molecular weight polypeptides (L chains) obtained by reductive cleavage of his myeloma proteins. Indeed, Putnam (2) has shown that peptide maps of the tryptic digests of oxidized Bence Jones proteins correspond to a portion of the peptide map of similarly treated autologous serum myeloma protein.Edelman and Benacerraf (3) have postulated that the manufacture of the L polypeptide chains is asynchronous in multiple myeloma, and thus a part of the cell output appears in the urine as Bence Jones protein, whereas other chains are incorporated into the circulating myeloma globulin. It was of interest, therefore, to examine the uncommon instance of Bence Jones proteinuria in a patient with Waldenstrdm's macroglobulinemia and particularly to compare the L chains of the serum macroglobulins and y2-globulins with the urinary Bence Jones protein.Evidence is presented to show that the Bence Jones protein is chemically and antigenically similar to the L chain derived from the patient's macroglobulin and antigenically deficient when compared to the L chain of the autologous 7 S y2-globulin.Materials and Methods Clinical informationt. The patient in the present study, a 74-year-old Caucasian male, was admitted to the Ear, Nose, and Throat Service of the University of California * Submitted for publication July 16, 1963; accepted September 19, 1963. Supported in part by grants A-1229 and B-1099 from the National Institutes of Health, Bethesda, Md., a grant from The National Foundation, and funds from the Research Committee of the University of California School of Medicine.Medical Center, in January 1963, because of gradual, progressive loss of hearing during the preceding year. He had always been in excellent health except for several episodes of unexplained epistaxis one year before admission. In the course of the initial physical examination, hepatomegaly was detected, and initial laboratory studies revealed a 3 + proteinuria positive for Bence Jones protein and a normochromic, normocytic anemia with marked rouleaux formation. Additional laboratory studies showed a hemoglobin of 9.3 g per 100 ml, hematocrit of 29%, and leukocyte count of 5,100 per mm'. The total serum protein was 11.4 g per 100 ml; serum electrophoretic analysis showed 20% albumin and 61% y-globulin. A Sia test showed a 4+ reaction. Bone marrow aspiration detected lymphocytosis and plasmacytosis, and an X-ray bone survey demonstrated generalized demineralization.Materials. The sodium salts of reagent grade phosphate and acetate were used for the preparation of the buffers; reagent grade urea was used. Additional materials were mercaptoethanol,1 iodoacetamide,2 carboxymethyl-cellulose (CM-cellulose, 0.8 mEq per g),3 and diethylaminoethyl-cellulose (DEAE-cellulose, 0.9 mEq per g).3 The exchangers were recycled through acid and base washes before use. Also used were cross-linked dextran (140 to 400 mesh) 4 and a crystalline prep...

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“…7S71 antibodies apparently do not bind complement in vitro in the presence of antigen nor do they hemolyze antigencoated, tanned erythrocytes in the presence of complement. Since complement fixation (3) and binding to sites in guinea pig tissues are dependent on properties of fragment III of Porter (16) and therefore of H chains (17), it must be assumed that, for the guinea pig antibody studied, a given H chain does not possess both properties.…”

Section: Discussionmentioning

confidence: 99%

Properties of Guinea Pig 7s Antibodies

Bloch

Kourilsky

Óváry

et al. 1963

The Journal of Experimental Medicine

189

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In the preceding papers (1, 2) it was demonstrated that guinea pigs immunized with single proteins or protein-hapten conjugates produced two major types of antibodies differing in their electrophoretic mobility. These antibodies were identified as 71 and 7~; both had a sedimentation coefficient of approximately 7S. Gamma-1 or "fast" migrating antibodies conferred passive cutaneous and systemic anaphylactic reactions in guinea pigs; gamma-2 or "slow" migrating antibodies did not mediate these activities.The present report is concerned with the ability of slow and fast guinea pig antibodies to fix complement in ~tro in the presence of antigen and to participate in certain in vivo reactions, which apparently involve the fixation of complement. It has been found that 7, antibodies bind complement in the presence of antigen and that 71 antibodies fail to do so. These differences may depend on the presence of a complement-fixing site on piece III of 7~ antibodies and the absence of this site from piece III of 71 antibodies (3). The slow antibody components of guinea pig antisera were found to be very effective in conferring passive Arthus reactivity (in the guinea pig), whereas fast components were relatively ineffective. These data suggest that complement activity is involved in the mechanism of the Arthus reaction.Studies of guinea pig anti-sheep erythrocyte sera demonstrated, in addition to the usual slow and fast antibodies, a highly efficient hemolysin of intermediate electrophoretic mobility. Whether this activity is a function of a third type of antibody, which is perhaps produced in response to the particulate properties of the antigen, or to antigenic heterogeneity of the red cell membrane, remains to be determined.

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

Cited by 79 publications

References 20 publications

Structure and Specificity of Guinea Pig 7s Antibodies

Structure and Specificity of Guinea Pig 7s Antibodies

Macroglobulinemia with Bence Jones Proteinuria: Comparison of Urinary Protein and L Chain of Serum Proteins*

Properties of Guinea Pig 7s Antibodies

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