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PMID: 111247 Published · ppublish English Journal Article

Amino acid sequence of a mouse immunoglobulin mu chain.

Kehry M, Sibley C, Fuhrman J, Schilling J, Hood LE

Abstract

The complete amino acid sequence of the mouse mu chain from the BALB/c myeloma tumor MOPC 104E is reported. The C mu region contains four consecutive homology regions of approximately 110 residues and a COOH-terminal region of 19 residues. A comparison of this mu chain from mouse with a complete mu sequence from human (Ou) and a partial mu chain sequence from dog (Moo) reveals a striking gradient of increasing homology from the NH2-terminal to the COOH-terminal portion of these mu chains, with the former being the least and the latter the most highly conserved. Four of the five sites of carbohydrate attachment appear to be at identical residue positions when the constant regions of the mouse and human mu chains are compared. The mu chain of MOPC 104E has a carbohydrate moiety attached in the second hypervariable region. This is particularly interesting in view of the fact that MOPC 104E binds alpha-(1 leads to 3)-dextran, a simple carbohydrate. The structural and functional constraints imposed by these comparative sequence analyses are discussed.

MeSH Terms
Amino Acid Sequence Animals Cell Line Immunoglobulin Fragments/analysis Immunoglobulin Heavy Chains Immunoglobulin M Immunoglobulin mu-Chains Mice Oligosaccharides/analysis Plasmacytoma
Chemicals
Immunoglobulin Fragments Immunoglobulin Heavy Chains Immunoglobulin M Immunoglobulin mu-Chains Oligosaccharides
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Kehry M
Sibley C
Fuhrman J
Schilling J
Hood L E
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39 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1979-06-00
Pages
2932-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC383724
Subset
IM
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