plasmacytoma/carbohydrate

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Characterization of the antibody to the C-carbohydrate produced by a transplantable mouse plasmacytoma.

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[The disorder of carbohydrate metabolism as a result of diamidine therapy of plasmocytoma].

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Hybridomas specific for carbohydrates; synthetic human blood group antigens for the production, selection, and characterization of monoclonal typing reagents.

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A general method for the production of carbohydrate-specific hybridoma antibodies is illustrated by generation of monoclonal antibody to the antigenic determinant of human blood group B. This trisaccharide determinant was chemically synthesized and covalently coupled to bovine serum albumin and

Isolation, purification, and characterization of a mouse plasmacytoma cell surface glycoprotein involved in the resistance of the tumor cells to immune destruction.

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Cells of a subline of the mouse plasmacytoma LPC-1 are resistant to lysis by cytotoxic T-lymphocytes, probably as a result of the blocking of the major histocompatibility gene complex-encoded cell surface antigens by a trypsin-sensitive glycoprotein of approximately 160 kilodaltons. This

Involvement of carbohydrate moieties in the expression of effector activity of cytotoxic T cells against syngeneic tumor cells.

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Cytotoxic T lymphocytes (CTL) were raised against syngeneic plasmacytoma MOPC-315 cells by culturing spleen cells immunized with MOPC-315 cells 7 to 14 days previously, in the presence of MOPC-315 cells for 5 days. The cytotoxic activity of these CTL was blocked by D-mannose, indicating that

Plasmacytomas of the NZB mouse.

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Plasmacytomas were readily induced in NZB mice by three i.p. inoculations with pristane (2, 6, 10, 14-tetramethylpentadecane). In comparison with comparable induction regimens in BALB/c mice a) the latent period for plasmacytoma development was significantly longer in NZB's; b) the frequency of IgA

Microheterogeneity of Immunoglobulin G from plasmocytomas. Identification of two types of IgG by isoelectric focusing.

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Isoelectric focusing of serum immunoglobulin G (IgG) revealed that the microheterogeneity, which is expressed in the isoelectric points (IEP), partly is caused by differences in the content of N-acetyl-neuraminic acid (NANA), partly by other effects, probably including deamidation. Two different

Ten percent of normal B cells and plasma cells share A VH determinant(s) (J606-GAC) with a distinct subset of murine VHIII plasmacytomas.

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Our findings indicate that a subset of VHIII antibodies, which we refer to as J606-GAC, contains a determinant(s) that is present on 5 to 15% of normal splenic B cells and plasma cells as detected by immunofluorescence. This subpopulation is detected by purified antibody, 0-1, which was prepared

Heterogeneity of asparagine-linked oligosaccharides of five glycosylation sites on immunoglobulin M heavy chain from mineral oil plasmacytoma 104E.

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Mouse myeloma immunoglobulin IgM heavy chains were cleaved with cyanogen bromide into nine peptide fragments, four of which contain asparagine-linked sites of glycosylation. Three of these glycopeptides contain a single site located at asparagines 171, 403, and 563 in the sequence of the intact

Glycosylation is not required for membrane localization or secretion of IgM in a mouse B cell lymphoma.

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We have investigated the importance of glycosylation in determining the function of membrane-bound and secreted immunoglobulin M (IgM). Hickman and Kornfeld (1978) previously observed that glycosylation is required for IgM to be secreted by 104E, a mouse plasma cell tumor. In order to determine

Mouse intracellular immunoglobulin M. Structure and identification of a free thiol group.

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Monomeric intracellular mouse immunoglobulin M (hereafter designated IgMs) was purified in milligram quantities from the plasma cells of mouse plasmacytoma MOPC 104E after lysis either in the presence or in the absence of iodoacetate. Peptide ;mapping' analysis of the IgMs after partial reduction

Addition of glucosamine and mannose to nascent immunoglobulin heavy chains.

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We have investigated the process of protein glycosylation in an attempt to answer the question of whether glucosamine and mannose are added to nascent chains prior to chain completion or only to completed chains after release from the ribosome. The MPC 11 mouse plasmacytoma cell line used in these

Effect of glycosylation inhibitors on the structure and function of the murine transferrin receptor.

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The murine transferrin receptor is a disulphide-linked dimer with three N-glycosylation sites. We have investigated the structural and functional properties of the transferrin receptor from murine plasmacytoma cells (NS-1 cells) treated with the glycosylation inhibitor, tunicamycin and the

Processing of MOPC 315 immunoglobulin A oligosaccharides: evidence for endoplasmic reticulum and trans Golgi alpha 1,2-mannosidase activity.

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The processing of asparagine-linked oligosaccharides on the alpha-chains of an immunoglobulin A (IgA) has been investigated using MOPC 315 murine plasmacytoma cells. These cells secrete IgA containing complex-type oligosaccharides that were not sensitive to endo-beta-N-acetylglucosaminidase H. In

Glycoprotein biosynthesis in myeloma cells. Characterization on nonglycosylated immunoglobulin light chain secreted in presence of 2-deoxy-D-glucose.

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The biosynthesis and secretion of a glycosylated, K-type immunoglobulin light chain (K-46) was studied in a mouse myeloma tumor, mineral oil plasmacytoma-46B. Viable single cell suspensions were prepared from excised tumors and optimal conditions were established for incorporation of amino acid and

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