Binding properties of a mouse immunoglobulin M myeloma protein with carbohydrate specificity

Young, N. Martin; Jocius, Irene B.; Leon, Myron A.

doi:10.1021/bi00794a022

Cited by 65 publications

(18 citation statements)

References 18 publications

(13 reference statements)

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“…For instance, we estimated IgM of MOPC-104E to have <1% of its H chains as #' chains. This is consistent with previous data showing each IgM pentamer of 104E to have 10 homogeneous binding sites (14). Further, H chains of the 104E IGM have been isolated and sequenced, and no truncated # chains were noted (1 I).…”

Section: Implications Of#' Chains For Igm Valence the Presence Of U'supporting

confidence: 91%

“…The tumor IgM proteins of MOPC-104E (104E), K6100.16 (6100), HPCM3 (M3), and HPCM27 (M27) were specifically purified on the basis of their known binding specificities: 104E (14) was precipitated with a 1-3 dextran; 6100 (28) was precipitated with NP [(4-hydroxy-3-nitrophenyl)acetyl]-conjugated bovine serum albumin; and M3/M27 (29) were affinity purified by absorption onto PC-conjugated Affigel beads followed by elution with l0 -3 M PC. These preparations are designated 104E(dx), 6100(NP), M3(PC), and M27(PC), respectively.…”

Section: Methodsmentioning

confidence: 99%

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Truncated mu (mu') chains in murine IgM. Evidence that mu' chains lack variable regions.

Marks¹,

Bosma²

1985

The Journal of Experimental Medicine

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Secreted IgM was shown to contain truncated mu (mu') chains with an apparent molecular mass of approximately 55 kD. The estimated percentage of IgM heavy (H) chains in the mu' form ranged from less than or equal to 1% in the case of one tumor IgM protein (104E) to greater than or equal to 30% in normal serum IgM. Serum mu' chains lacked antigenic determinants characteristic of immunoglobulin variable regions and showed a restricted isoelectric focusing pattern compared with that of conventional mu chains. Intracellular mu' chains were readily detected in bone marrow cells but not in spleen or lymph node cells; mu' chains were also detected in IgM-producing tumor cells and in a hybridoma cell line that deleted its productive mu allele. These results predict irregularities in IgM structure and recall an old controversy concerning the valence of IgM molecules.

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Section: Implications Of#' Chains For Igm Valence the Presence Of U'supporting

confidence: 91%

Section: Methodsmentioning

confidence: 99%

Truncated mu (mu') chains in murine IgM. Evidence that mu' chains lack variable regions.

Marks¹,

Bosma²

1985

The Journal of Experimental Medicine

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“…J558 (13) and MOPC104E (12), while demonstrating specificity for a-1,3-linked oligosaccharides, are different as shown by the analysis of inhibition of dextran binding of these proteins by various nigerosyl derivatives. One explanation for the idiotypic difference between these proteins could be that they share certain idiotypic determinants in common, while differing in others.…”

Section: Specificity Of Anti-idiotypic Antibodiesmentioning

confidence: 94%

“…Since both MOPC104E and J558 have specificity for a-1,3-linked oligosaccharides (12,13), it was of particular interest to test MOPC104E for crossreaction with the J558 idiotype by the radioimmunoassay. As shown in Fig.…”

Section: Specificity Of Anti-idiotypic Antibodiesmentioning

confidence: 99%

Immunochemical Analysis of the Cross-Reacting Idiotypes of Mouse Myeloma Proteins with Anti-Dextran Activity and Normal Anti-Dextran Antibody

Carson

Weigert

1973

Proc. Natl. Acad. Sci. U.S.A.

122

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The idiotype of the mouse myeloma protein with anti-a-1,3 dextran activity, J558, has been characterized by a solid-phase radioimmunoassay. The idiotype of the J558 protein depends on a specific light and heavy chain interaction and is altered in the presence of the hapten, nigerose. Cross-reacting idiotypes were found on another mouse myeloma protein with a-1,3 dextran specificity, normal anti-dextran antibody, and certain reconstructed myeloma proteins composed of the J558 heavy chain and heterologous light chains.The immune response to a-1,3-linked dextrans in mice is controlled by an autosomal dominant locus linked to the genes of the constant region of the heavy chain. This locus determines the level of the response to dextrans containing a-1,3 glucosyl linkages, as well as the structure of the antibody. Certain strains that respond well to this antigen produce anti-dextran antibody restricted to the X class. Most or all anti-dextran antibodies share an antigenic determinant(s) (idiotype) that occurs on a 'yAX BALB/c myeloma immunoglobulin with specificity for a-1,3-linked dextrans. Thus, this idiotype provides a marker for the antibody variable region that is coded for by the locus controlling the dextran response (1).In this study, we show that this idiotype is dependent on variable regions of both heavy and light chains; and that the idiotype of the antibodies to the dextrans is related to their specificity, as demonstrated by studies on the influence of hapten, and the effect of amino-acid differences in the complementarity-determining regions of anti-dextran antibodies on the idiotype.

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“…2. All proteins carrying the H8s determinant (43) are indistinguishable with respect to either their affinity for phosphorylcholine (46) eEach of these proteins also has unique V-region determinants.…”

Section: Idiotypymentioning

confidence: 99%

The Biological Origin of Antibody Diversity

Williamson¹

1976

Annu. Rev. Biochem.

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Antibody diversity has a compelling fascination for many scientists and over the years speculations have sometimes seemed more numerous than facts. Now the structural basis of antibody specificity is well defined. Amino acid sequences and recently three-dimensional structures of various immunoglobulins provide the most solid basis for discussing the origin of diversity. The novel pattern of variable (V) and Constant (C) regions of amino acid sequence has been resolved further to show the functional pattern of variability. Inheritance of separate V and C genes is accepted, but attempts to define more than one gene coding for each V region are considered here to be unnecessary. The pattern of variability is still best understood in terms of mutation and the presence or absence of various selective pressures. The major area of debate still hinges around the extent to which mutation and selection operate during evolution or somatically. Sequence data have now been generally interpreted to require multiple V genes carried in the germ line. A few individual VH genes have been mapped in close linkage to CH genes in the mouse. The apparent existence of three VH alleles in rabbits was a strong argument against multiple V genes. Now the three phenotypes have been shown to be due to alleles controlling the expression of three sets of VH genes all present on the same chromosome. That V-gene expression requires rejoining of V and C genes at the DNA level is now almost certain. Models for the joining process can draw on the precedents of transposable genetic elements, which are widespread in Nature. The total extent of antibody diversity remains a philosophical point. Estimates of the number of antibody molecules required for observed diversity are reduced by two recently documented proposals. Each antibody combining site apparently has many (estimated at 100) different specificities and most combinations of VH and VL regions probably form a viable site. A given combining site can be defined by its pattern of shared specificities. Several specific antibody repertoires have been measured and the size in each case is consistent with the stringency with which the specificity is selected. Repertoire size appears to be under genetic control, but there are problems in viewing the genotype through the veil of clonal selection. Molecular hybridization has been used recently in an attempt to count V and C genes directly. C genes are seen in DNA having nonreiterated sequences, as formal genetics predicts. Each V-region probe hybridizes at a similar rate to C-region probes. Interpretation of this result depends on the extent to which one V-region probe will reveal nonhomologous V genes. Previous estimates that many cross-hybridizing genes should have been seen if present are possibly exaggerated. It is argued here that the data are compatible with a germ-line gene for each probe studied. Maximum estimates for the number of germ-line genes are sufficient to account for antibody diversity...

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Binding properties of a mouse immunoglobulin M myeloma protein with carbohydrate specificity

Abstract: The IgM protein from the murine plasmacytoma MOPC 104E was prepared by a simple immunospecific procedure involving precipitation by dextran, dissociation by hapten, and anion-exchange chromatography. The binding

Cited by 65 publications

References 18 publications

Truncated mu (mu') chains in murine IgM. Evidence that mu' chains lack variable regions.

Truncated mu (mu') chains in murine IgM. Evidence that mu' chains lack variable regions.

Immunochemical Analysis of the Cross-Reacting Idiotypes of Mouse Myeloma Proteins with Anti-Dextran Activity and Normal Anti-Dextran Antibody

The Biological Origin of Antibody Diversity

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