scholarly journals TWO TYPES OF γ-MYELOMA PROTEINS, β2A-MYELOMA PROTEINS, γ1-MACROGLOBULINS, AND BENCE JONES PROTEINS IDENTIFIED BY TWO GROUPS OF COMMON ANTIGENIC DETERMINANTS

1963 ◽  
Vol 42 (6) ◽  
pp. 811-822 ◽  
Author(s):  
John L. Fahey ◽  
Alan Solomon
Keyword(s):  
Antigenic Determinants ◽  
Myeloma Proteins ◽  
Bence Jones Proteins

scholarly journals CLASSIFICATION OF MYELOMA PROTEINS, BENCE JONES PROTEINS, AND MACROGLOBULINS INTO TWO GROUPS ON THE BASIS OF COMMON ANTIGENIC CHARACTERS

1962 ◽  
Vol 116 (6) ◽  
pp. 859-877 ◽  
Author(s):  
Mart Mannik ◽  
Henry G. Kunkel
Keyword(s):  
Multiple Myeloma ◽  
Antigenic Determinants ◽  
General Category ◽  
Myeloma Protein ◽  
Myeloma Proteins ◽  
Protein Molecules ◽  
Bence Jones Proteins

Antisera to normal 7S γ-globulin and to Bence Jones proteins permit the grouping of myeloma proteins (gamma and beta 2A types), Bence Jones proteins, and the Waldenström type macroglobulins into two fundamental antigenic groups. The antigenic determinants responsible for this grouping are common to all these proteins which fall in the general category of immunoglobulins. Antisera to Bence Jones proteins were particularly useful for this classification since they failed to react with the proteins of the opposite group. These antisera also permit the grouping of normal 7S γ-globulin into two major types. The Bence Jones proteins from individual patients were found to correspond in antigenic group to that of the serum myeloma protein. Studies with antisera to 7S γ-globulin and to Bence Jones proteins indicated that the Bence Jones proteins were antigenically identical to a portion of the corresponding multiple myeloma protein molecules.

scholarly journals TWO MAJOR TYPES OF NORMAL 7S γ-GLOBULIN

1963 ◽  
Vol 117 (2) ◽  
pp. 213-230 ◽  
Author(s):  
Mart Mannik ◽  
Henry G. Kunkel
Keyword(s):  
Multiple Myeloma ◽  
Antigenic Determinants ◽  
Myeloma Proteins ◽  
Group 2 ◽  
Group 1 ◽  
Bence Jones Proteins

Normal 7S human γ-globulin was found to contain two fundamental antigenic groups of molecules. The group 1 molecules of normal γglobulin correspond antigenically to group 1 multiple myeloma proteins and Bence Jones proteins; and group 2 molecules of normal γ-globulin correspond antigenically to group 2 multiple myeloma proteins and Bence-Jones proteins. Among pooled human Fr II and several individual γ-globulin preparations, approximately 60 per cent of molecules belong to group 1 and approximately 30 per cent of molecules to group 2 in this classification. The possible existence of a third minor antigenic group, constituting about 10 per cent, is discussed. Antisera to Bence Jones proteins of antigenic group 1 and group 2, in conjunction with I-131-labeled 7S γ-globulin proved to be the most useful system for defining the antigenic groups of normal γ-globulin. The group-specific antigenic determinants of normal 7S γ-globulin molecules were located on the S fragments of these proteins.

scholarly journals IMMUNOLOGICAL STUDIES OF HUMAN γ-GLOBULIN

1960 ◽  
Vol 112 (1) ◽  
pp. 203-223 ◽  
Author(s):  
G. M. Edelman ◽  
J. F. Heremans ◽  
M.-Th. Heremans ◽  
H. G. Kunkel
Keyword(s):  
Deae Cellulose ◽  
Antigenic Determinants ◽  
Agar Diffusion ◽  
Myeloma Proteins ◽  
Zone Electrophoresis ◽  
Γ Globulins

Two major antigenic fragments were obtained from various purified γ-globulin preparations after papain treatment. One, the F component, had a mobility faster than the original γ-globulin and the second, the S component, had a slower mobility. Similar F and S components were also obtained with certain homogeneous myeloma proteins which were closely related to γ-globulin immunologically. Additional minor antigenic components were detected with certain antisera. The technique of immunoelectrophoresis was particularly useful for bringing out the different antigenic constituents obtained after papain treatment. The F and S components as well as a midfraction were isolated by chromatography on DEAE-cellulose. These were immunologically homogeneous and could be utilized to absorb F and S antibodies from various antisera. The relative amount of F and S antibodies varied in different antisera from individual rabbits immunized with whole γ-globulin. Whole γ-globulin was separated by zone electrophoresis into a fast migrating and a more slowly migrating fraction. Each of these gave rise to F and S components after splitting with papain. The F components of the two γ-globulins were similar in mobility, while the S components showed marked mobility differences although antigenically they were very similar. The mobility differences of the parent γ-globulin appeared to be primarily related to the differences in the S component. Certain antisera against pathological γ-globulins were found to give double lines with a wide variety of γ-globulin preparations in agar diffusion. These were shown to be related to the F and S antigenic determinants of γ-glubulin. This relationship was evident by a number of procedures utilizing both Ouchterlony plate techniques and immunoelectrophoresis. The question of whether these findings indicate heterogeneity of γ-globulin in relation to the F and S antigenic components, or whether different antigenic groups on one molecule can give rise to separate lines in certain instances, is discussed.

scholarly journals COMMON INDIVIDUAL ANTIGENIC DETERMINANTS IN FIVE OF EIGHT BALB/c IGA MYELOMA PROTEINS THAT BIND PHOSPHORYL CHOLINE

1970 ◽  
Vol 132 (4) ◽  
pp. 737-751 ◽  
Author(s):  
Michael Potter ◽  
Rose Lieberman
Keyword(s):  
Single Species ◽  
Inbred Strains ◽  
Antigenic Determinants ◽  
Fab Fragments ◽  
Phosphoryl Choline ◽  
Myeloma Proteins ◽  
Highly Sensitive ◽  
Specific Antisera ◽  
Related Proteins

Eight IgA myeloma proteins derived from independently induced plasma-cytomas in genetically similar inbred BALB/c mice are functionally related by their binding of phosphoryl choline-containing antigens (Pneumococcus C polysaccharide or Lactobacillus antigen). Each protein resembles a single species of immunoglobulin in antibody. The proteins are characterized by highly sensitive myeloma-specific antisera prepared by immunizing mice of other inbred strains with the BALB/c myeloma proteins. Individual or myeloma-specific determinants located on Fab fragments were found on three of the proteins that were unique for that protein and did not react with any other IgA protein among over 70 tested. Remarkably, five of the proteins shared two common myeloma-specific determinants which were specific for this group of five proteins. These results suggest that the five functionally and genetically related proteins sharing the same myeloma-specific determinants might also be structurally similar.

scholarly journals IMMUNOCHEMICAL STUDIES OF TWENTY MOUSE MYELOMA PROTEINS: EVIDENCE FOR TWO GROUPS OF PROTEINS SIMILAR TO GAMMA AND BETA-2A GLOBULINS IN MAN

1961 ◽  
Vol 114 (3) ◽  
pp. 385-398 ◽  
Author(s):  
John L. Fahey
Keyword(s):  
Plasma Cell ◽  
Plasma Cells ◽  
Strain Differences ◽  
Normal Serum ◽  
Antigenic Determinants ◽  
Mouse Strains ◽  
Mouse Plasma ◽  
Myeloma Proteins ◽  
Beta Globulin ◽  
Mouse Myeloma

The serum myeloma proteins associated with 20 mouse plasma cell tumors in C3H or BALB/c mice that had proved transplantable were characterized by electrophoretic and immunochemical techniques. Although the myeloma proteins ranged in electrophoretic mobility from gamma to alpha globulins, they could be divided into two groups, the gamma type and the beta type myeloma globulins, on the basis of characteristic immunochemical properties. Gamma type myeloma proteins (5563, MPC-11) showed a close immunochemical relationship to normal mouse gamma globulins. Eighteen beta type mouse myeloma proteins migrated as beta or alpha globulins on zone electrophoresis. These proteins shared common antigenic features which permitted their recognition, separate from gamma myeloma proteins. The beta type myeloma proteins were shown to be related to a beta globulin component present in normal serum. Strain differences were observed for the normal beta globulin component believed to be formed in plasma cells. The proteins formed in mouse plasma cells were found to be antigenically complex. Shared antigenic determinants as well as distinctive antigenic determinants were detected when representative myeloma proteins were purified and compared by the Ouchterlony double diffusion technique. The myeloma proteins associated with each of the transplantable plasma cell tumors in mice are regarded as distinctive and characteristic products of plasma cell metabolism. The variety of myeloma globulins was similar for plasma cell tumors arising in C3H as well as in BALB/c mice, indicating that differences in mouse strains would not account for the differences among the myeloma globulins. These differences, however, may be due to differences among the normal plasma cells from which the malignant cells are derived. If this is so, the variety of myeloma globulins reflect the variety of plasma cells present normally.

scholarly journals Binding properties of immunoglobulin combining sites specific for terminal or nonterminal antigenic determinants in dextran.

1975 ◽  
Vol 142 (2) ◽  
pp. 435-459 ◽  
Author(s):  
J Cisar ◽  
E A Kabat ◽  
M M Dorner ◽  
J Liao
Keyword(s):  
Binding Energy ◽  
Large Fraction ◽  
Binding Constants ◽  
Antigenic Determinants ◽  
Low Molecular Weight ◽  
Total Binding Energy ◽  
Binding Properties ◽  
Total Binding ◽  
Myeloma Proteins ◽  
Mouse Myeloma

Binding constants of the dextran-reactive BALB/c mouse IgA myeloma proteins W3129 and QUPC 52 have been determined for each member of the isomaltose series of oligosaccharides and for methyl alphaDglucoside. Protein W3129 has maximum complementarity for isomaltopentaose (IM5) deltaf degrees = 7,180 cal/mol) with 55-60% of the total binding energy directed against methylalphaDglucoside. Protein QUPC 52 gives maximum binding with isomaltohexaose (IM6) (deltaF degrees = -5,340 cal/mol) and has about 70% of its total binding energy for isomaltotriose (IM3), but at most only 5% for isomaltose (IM2) or methyl alphaDglucoside. Protein W3129 precipitates with branched dextrans high in alpha (1 yields 6) linkages and reacts with but does not precipitate a synthetic alpha (1 yields 6)-linked linear dextran. Protein QUPC 52 precipitates both branched and linear dextrans. Thus, the immunodominant group for protein W3129 is mimicked by methyl alphaDglucoside and this protein reacts exclusively at the terminal nonreducing ends of alpha (1 yields 6)-linked dextran chains. Protein QUPC 52 has an immunodominant group which is expressed by IM3 but not smaller oligosaccharides and this protein can react at nonterminal locations along alpha (1 yields 6)-linked dextran chains.Precipitation of linear dextran seems to be a valid although not quantitative assay for antidextrans with nonterminal specificity. Quantitative precipitin reactions with branched and linear dextrans suggest that alpha (1 yields 6)-specific human antidextrans are mixtures of molecules having terminal and nonterminal specificities and that the fraction of each type can vary among individuals. Rabbit antisera against IM3 or IM6 coupled to bovine serum albumin also appear to contain antibodies with nonterminal specificity for dextran chains although a large fraction has terminal specificity. Low molecular weight clinical dextran N-150N (congruent to 60,000) reacted more like linear dextran than like its parent native-branched dextran B512. This is thought to result from an abundance of nonterminal determinants in clinical dextran N-150N but a very small number of functional terminal determinants per molecule. An appreciation of terminal and nonterminal specificities and of the different immunodominant structures in isomaltosyl chains has proven to be of a great value in understanding the immunochemical reactions of dextrans. Moreover, certain previous findings with fructosan-reactive mouse myeloma proteins and human antilevans (55, 84) also suggest terminal and nonterminal specificities for levan chains.

scholarly journals ANTIGENIC RELATIONSHIPS BETWEEN IMMUNE GLOBULINS AND CERTAIN RELATED PARAPROTEINS IN MAN

1961 ◽  
Vol 114 (4) ◽  
pp. 521-533 ◽  
Author(s):  
Edward C. Franklin ◽  
Denis R. Stanworth
Keyword(s):  
Biological Properties ◽  
The Other ◽  
Antigenic Specificity ◽  
Myeloma Proteins ◽  
Antigenic Properties ◽  
Immune Globulins ◽  
Γ Globulins ◽  
Antigenic Relationships ◽  
Gel Diffusion ◽  
Bence Jones Proteins

The antigenic properties of normal 19S γ-globulin, pathologic macroglobulins, ß2A-myeloma proteins, and Bence Jones proteins have been compared with 7S γ-globulin and the small 3.5S units derived from it by gel diffusion precipitin techniques. These studies demonstrate that the determinant groups on the 7S γ-globulin molecule responsible for the cross-reaction with each of the other proteins are associated with the two fragments of 7S γ-globulin which have the antibody-combining sites. The antigenic specificity of the 7S γ-globulin which distinguishes it from each of these proteins is associated primarily with the fragment that is richest in hexose and can not combine with antigen. However when compared with certain of the paraproteins additional antigenic specificity was also found to reside in the fragments with antibody-combining activity. The finding of similar antigenic relationships in rabbit γ-globulins suggests that some of the biological properties associated only with the 7S γ-globulins and not with the other immune globulins may reside in the fragment which also carries the antigenic specificity of the protein.

scholarly journals A STUDY OF IMMUNOGLOBULIN STRUCTURE

1969 ◽  
Vol 130 (2) ◽  
pp. 401-415 ◽  
Author(s):  
R. Quattrocchi ◽  
D. Cioli ◽  
C. Baglioni
Keyword(s):  
Light Chain ◽  
Peptide Mapping ◽  
Gel Filtration ◽  
Antigenic Determinants ◽  
Minimal Size ◽  
Bence Jones Protein ◽  
Peptide Map ◽  
Peptide Maps ◽  
Similar Peptide ◽  
Bence Jones Proteins

102 human Bence Jones proteins have been purified by gel filtration, digested with trypsin, and analyzed by peptide mapping. In several cases Bence Jones "fragments", corresponding to the variable half of the corresponding proteins, were observed. The peptide maps of the proteins were compared to establish whether any identical proteins were present in the sample analyzed. No Bence Jones protein showed a peptide map identical to that of any other protein, although remarkable similarities in the peptide maps were observed for some proteins. Two proteins that gave very similar peptide maps were then examined in detail, by purifying and analyzing the tryptic peptides. It was then found that these two proteins differ in amino acid sequence in at least six positions. The probability of not finding two identical sequences by examining a sample extracted from populations of light chains of different sizes has been calculated. This has led to an estimate of the minimal size of the population of light chain sequences in humans. The number of light chain sequences appears to be at least a few thousand. Information on the frequency of Inv and Oz antigenic determinants and on the relative frequency of subtypes of K chains has been obtained. Proteins of KI subtype are found most frequently. The possibility that different subtypes may be predominant in different species is discussed in relation to the evolutionary arguments used in favor of the somatic theories on the origin of variability of immunoglobulin chains.

scholarly journals COMPARISONS OF BENCE-JONES PROTEINS AND L POLYPEPTIDE CHAINS OF MYELOMA GLOBULINS AFTER HYDROLYSIS WITH TRYPSIN

1963 ◽  
Vol 118 (1) ◽  
pp. 41-53 ◽  
Author(s):  
J. H. Schwartz ◽  
G. M. Edelman
Keyword(s):  
High Voltage ◽  
Two Dimensional ◽  
Bence Jones Protein ◽  
Myeloma Protein ◽  
Myeloma Proteins ◽  
Group I ◽  
Chain Fraction ◽  
Polypeptide Chains ◽  
High Voltage Electrophoresis ◽  
Bence Jones Proteins

L polypeptide chains of myeloma globulin and Bence-Jones protein isolated from the same patient were found to be identical after comparison of their tryptic hydrolysates by two-dimensional high voltage electrophoresis. The patterns of peptides from proteins belonging to antigenic group I differed markedly from those of proteins in antigenic group II. A partially purified H chain fraction was compared with L chains from the same myeloma protein. The tryptic hydrolysates yielded dissimilar patterns of peptides. These data indicate that γ-myeloma proteins contain two kinds of polypeptide chains, Hγ chains and either LI or LII chains. The L chains appear to be identical with those comprising the Bence-Jones protein from the same patient.

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