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PMID: 6817080 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Mutations affecting the structure and function of immunoglobulin M.

Molecular and cellular biology ·Vol. 2 ·No. 9 ·1982-09-00 ·Pages 1033-43

Shulman MJ, Heusser C, Filkin C, Köhler G

Abstract

Using a hybridoma cell line which secretes hapten-specific immunoglobulin M (IgM), we have isolated a variety of mutants which produce abnormal immunoglobulin. Immunoglobulin was tested for the size and composition of the component heavy and light chains and for variable and constant region related functional and serological activities. Some mutants secrete IgM which seems to be defective in hapten binding; others make IgM which appears not to activate complement. Many of the mutants secrete monomeric as opposed to pentameric IgM. In some cases, the defect apparently correlates with structural alterations in the mu heavy chain: partial deletion, polypeptide addition, and abnormal glycosylation have been observed. These mutant cell lines provide a means of identifying the structural basis of IgM function and of studying the biochemistry of IgM synthesis and processing.

MeSH Terms
Animals Binding Sites, Antibody Complement Activation Hybridomas Immunoglobulin Constant Regions Immunoglobulin Heavy Chains Immunoglobulin Light Chains Immunoglobulin M/genetics,metabolism,physiology Immunoglobulin Variable Region Mice Mutation
Chemicals
Immunoglobulin Constant Regions Immunoglobulin Heavy Chains Immunoglobulin Light Chains Immunoglobulin M Immunoglobulin Variable Region
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Shulman M J
Heusser C
Filkin C
Köhler G
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49 references, click to expand
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
Published
1982-09-00
Pages
1033-43
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC369896
Subset
IM
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