The Primary Structure of μ-Chain-Disease Protein BOT. Peculiar Amino-Acid Sequence of the N-Terminal 42 Positions
- 1 January 1984
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 365 (1) , 105-118
- https://doi.org/10.1515/bchm2.1984.365.1.105
Abstract
The complete primary structure of the .mu. H-chain disease (.mu.-HCD) protein BOT was determined [in humans]. The monomeric HCD-.mu.-chain consists of 391 amino-acid residues, lacking the VH [H chain, variable part] and .mu.CH1 [1st domain of IgM H chain, constant part] domains but including the entire CH2, CH3 and CH4 domains (349 residues). The sequence of the preceeding 42 N-terminal residues which is designated as the pre-C-part presents no homology to any known variable or constant Ig sequence, but contains an internal homology of positions 10-19 to positions 20-29. The origin of the pre-C-part structure and the deletion of the .mu.CH1 domain of protein BOT are discussed.This publication has 21 references indexed in Scilit:
- Cellular myc oncogene is altered by chromosome translocation to an immunoglobulin locus in murine plasmacytomas and is rearranged similarly in human Burkitt lymphomas.Proceedings of the National Academy of Sciences, 1983
- Transcriptionally active c- myc oncogene is contained within NIARD, a DNA sequence associated with chromosome translocations in B-cell neoplasiaProceedings of the National Academy of Sciences, 1983
- Translocation of the c-myc gene into the immunoglobulin heavy chain locus in human Burkitt lymphoma and murine plasmacytoma cells.Proceedings of the National Academy of Sciences, 1982
- gamma Heavy chain disease in man: cDNA sequence supports partial gene deletion model.Proceedings of the National Academy of Sciences, 1982
- Chromatographie und Rechromatographie in der Hochdruckflüssigkeitschromatographie von Peptidgemischen. Die vollständige Primärstruktur einer Immunglobulin L-Kette vom κ-Typ, Subgruppe I (Bence-Jones-Protein Den)Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1981
- Präparative Auftrennung des tryptischen Hydrolysats eines Proteins mit Hilfe der Hochdruck-Flüssigkeitschromatographie. Die Primärstruktur einer monoklonalen L-Kette vom K-Typ, Subgruppe I (Bence-Jones-Protein Wes)Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1980
- Human heavy chain disease protein WIS: implications for the organization of immunoglobulin genes.Proceedings of the National Academy of Sciences, 1979
- Genetic determination of antibody specificityThe Science of Nature, 1978
- DEFECT IN MU HEAVY-CHAIN DISEASE PROTEIN GLI1976
- The Sequence Determination of a Protein in a Micro Scale: The Sequence Analysis of Ribosomal Protein L34 ofEscherichia coliHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1976