Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Protein 460 is a mouse myeloma gamma A(2) protein that competitively binds two small haptens, 2,4-epsilon-dinitrophenyl-L-lysine (Dnp-Lys) and 2-methyl-1:4-naphthaquinone thioglycollate (MenTG), to the antibody-combining region. The intact protein has a relatively inaccessible sulfhydryl group on each heavy chain. When it is substituted with a bulky reagent the binding affinity for MenTG decreases, while the binding of Dnp-Lys remains the same. Guanidine.HCl selectively reduces binding of Dnp-Lys; dimethylsulfoxide selectively reduces binding of MenTG. Papain digestion of protein 460 followed by column chromatography gave two fractions: one contained both binding activities and the other contained the sulfhydryl group. The affinity for Dnp-Lys of the first fraction is the same as that of the whole molecule, while affinity for MenTG is decreased. Since selective alteration of one or the other binding activity can occur in different ways, it seems likely that even though the haptens compete with each other, there is some spatial separation between the groups of contact amino-acid residues involved in the binding of these two haptens. These findings do not support the hypothesis that an immunoglobulin molecule carries combining sites complementary only to a single hapten or to a structurally related series of haptens, but rather suggests that the antibody-combining site may be a polyfunctional region capable of binding several structurally dissimilar haptens. We discuss a mechanism whereby polyfunctional combining sites can give rise to an antibody population (immune serum) that has a high degree of specificity to a single hapten.
 ...
PMID:Contact regions for dinitrophenyl and menadione haptens in an immunoglobulin binding more than one antigen. 411 41

We have previously shown that myeloma-derived or serum-derived immunoglobulin could facilitate in vitro alloantigen recognition by immunocompetent thymus cells ('subset-I thymocytes'). The present report demonstrates the isolation of surface immunoglobulins from radiolabeled splenic B lymphocytes. Solubilized radiolabeled preparations of surface immunoglobulin are shown to bind in vitro to lymphoid cells, especially to immunocompetent thymus cells. Immunocompetent thymus cells (subset-I thymocytes preferentially bind more IgG than IgM. Papain digests of IgG are also bound by subset-I thymocytes; preferential binding of the Fc piece is observed. Although the binding of IgG or its pieces per se does not activate lymphoid cells in vitro a role for the binding of IgG during alloantigen recognition in vitro between immunocompetent thymus cells is demonstrated.
 ...
PMID:Binding of surface IgG by immunocompetent thymus cells. 697 26

By means of immunodiffusion and immunoelectrophoresis study has been made of antigenic relationships of Bence Jones proteins, and the three classes of normal and pathological immunoglobulins, 7S gamma, beta(2A), and beta(2M). All thirty-nine Bence Jones proteins studied could be classified into either one of two distinct antigenic types, A or B. Both types are related to the immunoelectrophoretically slow (S) fragment of a papain digest of normal gamma-globulin; B is related more closely than A, but neither has antigenic determinants in common with the fast (F) fragment. The 7S gamma myeloma globulins were either immunological type I or II. The papain digests of these proteins produced the S and F precipitin lines in immunoelectrophoresis but multiple bands in starch gel electrophoresis, especially in the F region. The S fraction of type I myeloma globulins is antigenically similar to Bence Jones protein of type B, and the S component of type II myeloma globulins has antigenic determinants in common with type A Bence Jones protein. Correspondingly, myeloma patients with type I globulins and proteinuria usually excrete type B Bence Jones proteins, whereas patients with type II excrete type A proteins. The F fragment is the part common to normal 7S gamma-globulin and types I and II myeloma globulins but is absent in beta(2A) and beta(2M) pathological globulins and in both types of Bence Jones proteins. Papain digests of beta(2A) myeloma globulins produced a single precipitin line in immunoelectrophoresis. beta(2A) myeloma globulins appeared to have two antigenic units, one in common with type B Bence Jones protein and normal gamma-globulin, and another specific to beta(2A). The beta(2A) myeloma patients excreted type B Bence Jones protein. The papain digest of a macroglobulin produced two precipitin lines, the faster of which had antigenic determinants in common with type B Bence Jones protein, the slower seemed specific for the macroglobulin. Five serum micromolecular globulins proved to be either type A or B Bence Jones proteins. From the above results, an antigenic map was constructed showing which determinants are shared and which are specific for normal 7S gamma-globulin, types I and II myeloma globulins, beta(2A) myeloma globulins, a macroglobulin, and types A and B Bence Jones proteins.
 ...
PMID:Antigenic relationships of Bence Jones proteins, myeloma globulins, and normal human gama-globulin. 1393 73

The unique myeloma protein from S. J., a patient with multiple myeloma, was isolated and characterized. It resembled other myeloma proteins in many respects. The S. J. myeloma protein migrated in a distinct peak in the slow beta-globulin region on zone electrophoresis, appeared as a single band on starch gel electrophoresis, and sedimented at 7.04S in the ultracentrifuge. Papain and cysteine treatment produced Fc (fast) and Fab (slow) fragments. Reduction and alkylation of the myeloma protein produced heavy and light chains in a ratio of approximately 3:1. The S. J. myeloma protein had type L (type II) light chains. These were antigenically similar to the Bence Jones protein also found in this patient. The S. J. myeloma protein was unique in the properties of its heavy chains. The myeloma protein (and its heavy chains and Fc pieces) did not contain antigenic determinants specific for IgG, IgA, or IgM. The myeloma protein (and its heavy chains), however, did contain antigenic determinants which are characteristic of a new class of immunoglobulin. The S. J. myeloma protein was unusual also in its effect on the metabolism of normal IgG and in the electrophoretic mobility of the Fc fragment produced by papain digestion. No evidence was obtained to indicate that the entire heavy polypeptide of the S. J. protein was a grossly abnormal product of malignant cell metabolism. The unique properties of the S. J. myeloma protein (and its heavy chains) are believed to represent, in large measure, properties to be found in a small part of the normal immunoglobulin population.
 ...
PMID:A NEW CLASS OF HUMAN IMMUNOGLOBULINS. I. A UNIQUE MYELOMA PROTEIN. 1425 82