The Primary Structure of the Constant Part of μ‐Chain‐Disease Protein BOT
- 1 October 1980
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 111 (1) , 275-286
- https://doi.org/10.1111/j.1432-1033.1980.tb06103.x
Abstract
The complete primary structure of the constant part of the .mu. chain disease protein, BOT, was established. It includes the whole CH2, CH3 and CH4 domains. Two amino acid changes were found, at positions 309 (Ser .fwdarw. Gly) and 333 (Val .fwdarw. Gly) (GAL numbering). In 2 additional monoclonal .mu. chains (SCO and CO), the same positions showed an amino acid variability. From these data it may be concluded that 4 types of .mu. chains exist in the human: GAL type with Ser-309 and Val-333; OU type with Gly-309 and Val-333. SCO type with Ser-309 and Gly-333; and BOT/CO type with Gly-309 and Gly-333. The meaning of this molecular polymorphism is discussed.This publication has 34 references indexed in Scilit:
- The complete amino-acid sequence of a canine MU chainMolecular Immunology, 1979
- Micro‐sequence analysis of peptides and proteins using 4‐NN‐dimethylaminoazobenzene 4′‐isothiocyanate/phenylisothiocyanate double coupling methodFEBS Letters, 1978
- Partial sequence determination of normal pooled human immunoglobulin MImmunochemistry, 1977
- Allotypes of mouse IgM immunoglobulinNature, 1977
- Immunochemical and biochemical study of a human Fcμ fragment (μ‐chain disease)European Journal of Immunology, 1975
- The inter‐chain disulfide bonds of a μ‐chain disease proteinFEBS Letters, 1974
- An allotypic marker on chicken immunoglobulin MEuropean Journal of Immunology, 1974
- Recognition of Two Distinct Groups of Human IgM and IgA Based on Different Binding to StaphylococciScandinavian Journal of Immunology, 1974
- Structure of immunoglobulin A. Cysteine-containing peptides of the α chain of an immunoglobulin A1 myeloma proteinBiochemistry, 1973
- Zur Strukturregel der Antikörper. Die Primärstruktur einer monoklonalen Immunglobulin-L-Kette vom ϰ-Typ, Subgruppe III (Bence-Jones-Protein Ti). I. Reinigung und Charakterisierung des ProteinsHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1972