Complete amino acid sequence of a mouse mu chain: homology among heavy chain constant region domains
- 1 October 1982
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 21 (22) , 5415-5424
- https://doi.org/10.1021/bi00265a006
Abstract
The complete amino acid sequence of the mouse .mu. chain secreted by the MOPC 104E myeloma tumor was determined. There are 4 constant region domains in the .mu. chain and a 20-residue COOH-terminal segment that plays a role in the polymerization of pentameric Ig M molecules. There are 6 sites of carbohydrate attachment in the MOPC 104E .mu. chain. Three complex-type and 2 high-mannose oligosaccharides are located in the .mu. chain constant region. The general type and location of carbohydrate moieties in the .mu. chain constant region are completely conserved between mouse and human .mu. chains. Homology in the location of carbohydrate structures on different classes of heavy chains is discussed.This publication has 4 references indexed in Scilit:
- Nucleotide sequence divergence of mouse immunoglobulin gamma 1 and gamma 2b chain genes and the hypothesis of intervening sequence-mediated domain transfer.Proceedings of the National Academy of Sciences, 1980
- Sequences at the somatic recombination sites of immunoglobulin light-chain genesNature, 1979
- [46] Acylation with dicarboxylic acid anhydridesPublished by Elsevier ,1972
- [13] Reduction of disulfide bonds in proteins with dithiothreitolPublished by Elsevier ,1972