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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
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
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 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
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
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
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
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
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
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
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
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
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