Mouse myeloma mutants blocked in the assembly, glycosylation and secretion of immunoglobulin

S. Weitzman, M. D. Scharff

Research output: Contribution to journalArticlepeer-review

38 Scopus citations


Two stable mutant cell lines derived from the MPC-11 mouse myeloma synthesize immunoglobulin with abnormal heavy chains and normal light chains. The mutant heavy chains have molecular weights of 38,000 to 42,000 (M3.11) and 50,000 (ICR 11.19) as compared to 55,000 of the wild type. The mutants demonstrate a variety of blocks in the assembly, glycosylation and secretion of immunoglobulin. (1) The wild type assembles and secretes 90% of its immunoglobulin primarily as H2L2 while M3.11 is partially blocked in the assembly of H2L2, and secretes approximately one half of its immunoglobulin as HL. ICR 11.19, with a more complete block in interchain disulfide bond formation, assembles less than 10% of its immunoglobulin into H2L2, has a block in secretion and degrades most of its immunoglobulin. (2) M3.11 uses only one of the two wild type pathways of assembly. Reduction of isolated H2L2 with 2-mercapthoethanol suggests an altered stability of the inter-H chain disulfide bonds in M3.11 as compared to the wild type immunoglobulin. (3) While the parent glycosylates all of its heavy chains, M3.11 does not attach any carbohydrate to 30 to 50% of its heavy chains. These non-glycosylated heavy chains are, nonetheless, assembled and secreted with similar kinetics to the glycosylated heavy chain.

Original languageEnglish (US)
Pages (from-to)237-252
Number of pages16
JournalJournal of Molecular Biology
Issue number2
StatePublished - Apr 5 1976

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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