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Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Two major antigenic fragments were obtained from various purified gamma-globulin preparations after papain treatment. One, the F component, had a mobility faster than the original gamma-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 gamma-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 gamma-globulin. Whole gamma-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 gamma-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 gamma-globulin appeared to be primarily related to the differences in the S component. Certain antisera against pathological gamma-globulins were found to give double lines with a wide variety of gamma-globulin preparations in agar diffusion. These were shown to be related to the F and S antigenic determinants of gamma-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 gamma-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.
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PMID:Immunological studies of human gamma-globulin. Relation of the precipitin lines of whole gamma-globulin to those of the fragments produced by papain. 1372 58

The relationship of Bence Jones protein (mol wt = 45,000) to a beta(2A)-myeloma protein (mol wt = 160,000) formed by the same mouse plasma cell tumor (MPC-2) was investigated. The beta(2A)-myeloma protein was split by treatment with papain and cysteine into fragments (S(20,w) = 3.7S), similar in size to the Bence Jones protein (S(20,w) = 3.6S). Two types of fragments with distinct antigenic groupings designated S and F, were present in the MPC-2 myeloma protein digest. These were partially separated by DEAE-cellulose chromatography. The Bence Jones protein was found to share antigenic determinants with S fragments from the MPC-2 beta(2A)-myeloma protein and with S fragments from gamma-globulins. Physicochemical observations indicated, however, that the Bence Jones protein was not identical to the globulin fragments produced by treatment with papain and cysteine. Comparison of the S and F fragments from beta(2A)- and gamma-globulins revealed that the antigenic features shared by the various globulins derived from plasma cells (gamma- and beta(2A)-myeloma proteins, the range of normal gamma-globulins) are largely properties of the S fragments, whereas the distinctive antigenic differences between the gamma- and beta(2A)-myeloma proteins were properties which appeared in the F fragments of the molecules.
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PMID:Enzymatically produced subunits of proteins formed by plasma cells in mice. II. beta2a-Myeloma protein and Bence Jones protein. 1386 10

Gamma globulin and antibody obtained from inbred C(3)H mice are split by papain and cysteine into fragments roughly one-third the size of the original Molecule (S(20,w) = 3.5S). The papain digests were characterized by starch gel electrophoresis and immunological methods. The highly heterogeneous fragments could be divided into two groups with distinct antigenic determinants (S and F), which were separated by DEAE ion-exchange cellulose chromatography. Approximately two-thirds of the fragments had S antigenic groupings and one-third had F antigenic groupings. These data are consistent with the view that mouse gamma globulin is split by papain and cysteine into three major fragments, two of which are of the S type and one of the F type. Antibody activity of the original molecule was present in the S fragments. Although the S fragments did not precipitate the antigen (hemocyanin) they were shown to bind antigen specifically in the manner of univalent antibodies. The S fragments of normal gamma-globulin were very heterogeneous with a broad spectrum of electrophoretic mobilities. Comparison of S fragments from slow and fast migrating globulins showed that the mobilities of the original gamma-globulin samples were largely reflected in the mobilities of their S fragments. Additional observations indicated that the F fragments also may help to determine the electrophoretic mobility of intact gamma-globulin molecules. S fragments of differing electrophoretic mobility were shown to have the same antigenic determinants, indicating that the structural differences responsible for the electrophoretic mobility differences were not involved in the antigenic groupings identified with rabbit antisera. The F fragments of normal gamma-globulin migrated more rapidly than the S fragments, were less heterogeneous, and showed several bands on starch gel electrophoresis. The F fragments differed antigenically from the S fragments, and had no antibody activity. Two groups of F fragments (F and F') were detected with some antisera. The gamma-myeloma protein (5563) formed in a C(3)H plasma cell tumor and similarly fragmented by treatment with papain and cysteine, produced much more discrete S and F components than were found in the normal gamma-globulin digest. The electrophoretic properties of the myeloma protein fragments were within the range observed for normal gamma-globulin fragments. Although the gamma-myeloma protein shares antigenic determinants with normal gamma-globulins it lacks some of the antigenic groupings present in the gamma-globulin preparation. Both S and F fragments from the myeloma protein share antigenic determinants with the corresponding fragments from normal gamma-globulin. In addition, both S and F fragments of normal gamma-globulin possess antigenic groupings not present in fragments of the gamma-myeloma protein, accounting for the antigenic deficiency observed on comparison of the gamma-myeloma protein with normal gamma-globulins.
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PMID:Enzymatically produced subunits of proteins formed by plasma cells in mice. I. gamma-Globulin and gamma-myeloma proteins. 1389 3

A new class of immunoglobulin, IgD, was identified in normal human serum by immunochemical technics. Antiserums prepared against the unique S.J. myeloma protein facilitated recognition of the related normal protein. IgD was shown to possess type K (I) and type L (II) light chain determinants, similar to those present in other classes of immunoglobulins. IgD does not possess determinants which are specific to IgG, IgA, or IgM. The IgD proteins possess their own specific antigenic determinants. IgD migrates in the fast gamma-region on immunoelectrophoresis. The properties on sephadex gel filtration and DEAE cellulose chromatography are described. IgD was found to have a median level of 0.03 mg/ml in 100 normal serums. The range of concentrations found in individual normal serums is much wider, however, than that of other classes of immunoglobulins. IgD, on the average, accounts for less than 1 per cent of the normal serum immunoglobulins.
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PMID:A NEW CLASS OF HUMAN IMMUNOGLOBULINS. II. NORMAL SERUM IGD. 1425 83

As IgM is the first isotype of antibody which appears in blood after initial exposure to a foreign antigen in the pattern of primary response, detection, and quantification of this molecule in blood seems invaluable. To approach these goals, generation, and characterization of a highly specific mAb (monoclonal antibody) against human IgM were investigated. Human IgM immunoglobulins were used to immunize Balb/c mice. Spleen cells taken from the immunized animals were fused with SP2/O myeloma cells using PEG (polyethylene glycol, MW 1450) as fusogen. The hybridomas were cultured in HAT containing medium and supernatants from the growing hybrids were screened by enzyme-linked immunosorbent assay (ELISA) using plates coated with pure human IgM and the positive wells were then cloned at limiting dilutions. The best clone designated as MAN-1, was injected intraperitoneally to some Pristane-injected mice. Anti-IgM mAb was purified from the animals' ascitic fluid by protein-G sepharose followed by DEAE-cellulose ion exchange chromatography. MAN-1 interacted with human IgM with a very high specificity and affinity. The purity of the sample was tested by SDS-PAGE and the affinity constant was measured (K(a) = 3.5 x 10(9)M(-1). Immunoblotting and competitive ELISA were done and the results showed that the harvested antibody recognizes a conformational epitope on the mu chain of human IgM and there was no cross-reactivity with other subclasses of immunoglobulins. Furthermore, isotyping test was done and the results showed the subclass of the obtained mAb which was IgG(1)kappa.
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PMID:Generation of a novel high-affinity monoclonal antibody with conformational recognition epitope on human IgM. 2016 78


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