scholarly journals Clonal nature of the immune response to phosphorylcholine (PC). V. Cross-idiotypic specificity among heavy chains of murine anti-PC antibodies and PC-binding myeloma proteins.

1975 ◽  
Vol 141 (5) ◽  
pp. 1073-1083 ◽  
Author(s):  
J L Claflin ◽  
J M Davie
Keyword(s):  
Heavy Chain ◽  
Antigenic Determinant ◽  
Variable Region ◽  
Antigenic Determinants ◽  
Genetic Origin ◽  
Heavy Chains ◽  
Myeloma Proteins ◽  
Kappa Chain ◽  
Clonal Nature ◽  
Mouse Myeloma

Seven mouse myeloma proteins with specificity for phosphorylcholine (PC) were found to share a common antigenic determinant. This group of proteins contained members which differed in genetic origin, heavy chain class, kappa-chain subgroup, individual antigenic determinants and specificity for choline analogues. The cross-idiotypic determinant, VH-PC, was antigenically similar in each of the proteins and was associated with the variable portion of the heavy chain in the region of the antibody combining site. Further studies showed that an indistinguishable determinant was present on IgM anti-PC antibodies isolated from all strains of mice tested regardless of histocompatibility or heavy chain allotype. In view of the finding that this cross-idiotypic determinant was not found on antibodies or myeloma proteins which lacked specificity for PC, the data strongly suggest that a particular heavy chain variable region has been preserved in all mouse antibodies with specificity for PC.

scholarly journals Sequence of the full-length immunoglobulin κ-chain of mouse myeloma MPC 11

1978 ◽  
Vol 171 (2) ◽  
pp. 337-347 ◽  
Author(s):  
G P Smith
Keyword(s):  
Variable Region ◽  
Full Length ◽  
Light Chains ◽  
Its Sequence ◽  
Heavy Chains ◽  
Immunoglobulin Kappa ◽  
N Terminus ◽  
Kappa Chain ◽  
Kappa Light Chains ◽  
Mouse Myeloma

MPC 11 mouse myeloma cells synthesize two immunoglobulin kappa light chains, coded by two separate genes. One of these Kappa-chains has no variable region and is degraded intracellularly. The other is a full-length kappa-chain contaning both variable and constant regions: this chain is secreted, both by itself and combined with heavy chains in molecules of immunoglobulin G. This paper reports the amino acid sequence of the myeloma MPC 11 full-length kappa-chain. The chain is unusual in having 12 extra residues at its N-terminus when its sequence is aligned with those of other mouse kappa-chains; no other anomalies were found in its sequence.

scholarly journals SIX BALB/c IgA MYELOMA PROTEINS THAT BIND ß-(1 → 6)-D-GALACTAN

1973 ◽  
Vol 138 (5) ◽  
pp. 1095-1106 ◽  
Author(s):  
Stuart Rudikoff ◽  
Elizabeth B. Mushinski ◽  
Michael Potter ◽  
C. P. J. Glaudemans ◽  
Michael E. Jolley
Keyword(s):  
Amino Acid ◽  
Affinity Chromatography ◽  
Heavy Chain ◽  
Antigenic Determinant ◽  
Amino Acid Sequences ◽  
The Other ◽  
Light Chains ◽  
Heavy Chains ◽  
Myeloma Proteins ◽  
Highly Sensitive

Six IgA myeloma proteins of BALB/c origin which bind antigens containing ß-(1 → 6)-D-galactan side chains have been isolated by affinity chromatography on galactoside-BSA-Sepharose columns. Partial amino acid sequences of of the light chains to residue Cys23 and the heavy chains to reside 30 were determined on the automated sequencer. No differences were found among the six VK sequences. Among some 50 partial VK sequences that have thus far been determined these six chains are the only ones thus far identified in this subgroup; at least 25 VK subgroups in the mouse have been identified so far. The heavy chain partial sequences were also very closely related but two differences were found. One protein differed from the other five by having isoleucine instead of leucine at position 5, a second protein differed from the others by having an unidentified amino acid at position 19. Using the highly sensitive inhibition of hemagglutination method it was found that each of the proteins possessed a unique inidividual antigenic determinant.

scholarly journals Allotypically related sequences in the Fd fragment of rabbit immunoglobulin heavy chains

1971 ◽  
Vol 124 (2) ◽  
pp. 301-318 ◽  
Author(s):  
L. E. Mole ◽  
S. A. Jackson ◽  
R. R. Porter ◽  
J. M. Wilkinson
Keyword(s):  
Heavy Chain ◽  
Immunoglobulin G ◽  
Sequence Variation ◽  
Variable Region ◽  
Related Sequence ◽  
Heavy Chains ◽  
Rabbit Immunoglobulin ◽  
Variable Section ◽  
Terminal Section ◽  
Constant Section

The sequence has been completed of the N-terminal 94 residues of the variable section of the Fd fragment of heavy chains from rabbit immunoglobulin G (IgG) of allotype As1. Most of the sequence of the same section from IgG of allotype Aa3 is also reported. These results, in conjunction with a substantial sequence of the variable region of allotype Aa2 reported elsewhere (Fleischman, 1971), show the presence of 16 positions (including six consecutive positions) in which the residue present correlates with the allotype. No allotype-related sequence variation has been found in the constant section of the Fd fragment. This evidence supports the view that two genes code for the heavy chain and it can be used as evidence in favour of somatic mutation as the origin of the variability in the sequence of the N-terminal section. The evolutionary origin of the ‘a’ locus allotypes of rabbit immunoglobulins remains obscure.

scholarly journals Loss of an individual idiotype on chemical modification. A strategy for assigning idiotypic determinants.

1981 ◽  
Vol 153 (5) ◽  
pp. 1275-1285 ◽  
Author(s):  
J Dickerman ◽  
B Clevinger ◽  
B Friedenson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Chemical Modification ◽  
Heavy Chain ◽  
Light Chains ◽  
Heavy Chains ◽  
Myeloma Proteins ◽  
Low Levels ◽  
The Individual ◽  
Complementary Strategy

Two dextran-binding myeloma proteins, J558 and Hdex 24, which possess the same individual idiotype (IdI) were diazotized to low levels (1-3.3 groups per subunit) with 1-[14C]-p-aminobenzoate. Both proteins lost the IdI idiotype under these conditions with most of the label incorporated on the heavy chains of each protein. When the diazotization ws carried out in the presence of the hapten 1-O-methyl-alpha-D-glucopyranoside the loss of idiotypic reactivity could be prevented for J558 but not for Hdex 24. Under these conditions most of the label was incorporated on the light chains of J558, but on the heavy chains of Hdex 24. For J558, these results show that a major determinant of the individual idiotype is within the hypervariable positions of the heavy chain. For Hdex 24 the determinant being modified is on the heavy chain but not involved in hapten binding. These results are consistent with previous work showing that J558 and Hdex 24 differ in amino acid sequence in the D and the J segments of the heavy chain and offer an alternative and complementary strategy for assigning idiotypic determinants.

scholarly journals A monoclonal antibody that detects a V kappa-TEPC15 idiotypic determinant cross-reactive with a Thy-1 determinant.

1981 ◽  
Vol 153 (5) ◽  
pp. 1068-1079 ◽  
Author(s):  
E Pillemer ◽  
I L Weissman
Keyword(s):  
T Lymphocytes ◽  
Antigenic Determinant ◽  
Cell Surface Molecules ◽  
Future Studies ◽  
Surface Molecules ◽  
Myeloma Proteins ◽  
Unusual Phenomenon ◽  
Lymphocyte Antigens ◽  
Classical Immunoglobulin ◽  
Mouse Myeloma

To identify T lymphocyte antigens with immunoglobulin-like determinants, we prepared rat anti-mouse T cell monoclonal antibodies and screened them against a panel of purified mouse myeloma proteins representing all isotypes of immunoglobulin. One hybridoma, designated 42-21, was found to detect a novel antigenic determinant shared by V kappa-TEPC15 and the Thy-1 molecule on all T lymphocytes. Although several explanations for this unusual phenomenon exist, it may imply some role for the Thy-1 molecule in antigen and/or mitogen recognition. In any event, future studies of idiotypes on T lymphocytes must consider the possibility that anti-idiotypic sera detect cell surface molecules unrelated to classical immunoglobulin.

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 The amino acid sequences of the Fd fragments of two human γ 1 heavy chains

1970 ◽  
Vol 117 (4) ◽  
pp. 641-660 ◽  
Author(s):  
E. M. Press ◽  
N. M. Hogg
Keyword(s):  
Amino Acid ◽  
Aspartic Acid ◽  
Heavy Chain ◽  
Variable Region ◽  
Amino Acid Sequences ◽  
Light Chains ◽  
Aspartic Acid Residue ◽  
Variable Regions ◽  
Heavy Chain Variable Region ◽  
Heavy Chains

The amino acid sequences of the Fd fragments of two human pathological immunoglobulins of the immunoglobulin G1 class are reported. Comparison of the two sequences shows that the heavy-chain variable regions are similar in length to those of the light chains. The existence of heavy chain variable region subgroups is also deduced, from a comparison of these two sequences with those of another γ 1 chain, Eu, a μ chain, Ou, and the partial sequence of a fourth γ 1 chain, Ste. Carbohydrate has been found to be linked to an aspartic acid residue in the variable region of one of the γ 1 chains, Cor.

scholarly journals DEMONSTRATION OF HEAVY AND LIGHT CHAIN ANTIGENIC DETERMINANTS ON THE CELL-BOUND RECEPTOR FOR ANTIGEN

1970 ◽  
Vol 132 (6) ◽  
pp. 1233-1249 ◽  
Author(s):  
Curla S. Walters ◽  
Hans Wigzell
Keyword(s):  
Heavy Chain ◽  
Light Chain ◽  
Immune Cells ◽  
Surface Structures ◽  
High Rate ◽  
Antigenic Determinants ◽  
Antigen Binding ◽  
Memory Cells ◽  
Humoral Antibody ◽  
Heavy Chains

High-rate antibody-forming cells and immunological memory cells can be selectively retained if filtered through a column coated with relevant antigen. This trapping can be blocked if the cells are incubated with an anti-immunoglobulin serum prior to column passage. A similar blocking is not observed when cells are treated with an anti-lymphocyte serum, thereby excluding the possibility that any antibodies combining with surface structures could cause this effect. By the use of antisera specific for heavy or light chain antigens, it was possible to locate such antigens in the antigen-binding receptor areas of immune cells. Criss-cross studies using antisera specific for gamma 1 or gamma 2a heavy chains showed that the membrane receptor has the same heavy chain as will be present in the eventual product of that cell, the humoral antibody.

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.

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