Characterization of human L type Bence-Jones proteins containing carbohydrate
| Autor: | Ely Kr, Jean L. Rossiter, Allen B. Edmundson, Sheber Fa, Hutson Nk, Nanne B. Simonds |
|---|---|
| Rok vydání: | 1968 |
| Předmět: |
Electrophoresis
Chemical Phenomena Stereochemistry Lysine Carbohydrates Biophysics Oligosaccharides Mannose Biochemistry Fucose chemistry.chemical_compound Neuraminic acid Humans Amino Acids Molecular Biology Glycoproteins chemistry.chemical_classification Glucosamine Binding Sites Galactose Hexosamines Oligosaccharide Glycopeptide Neoplasm Proteins Amino acid Chemistry chemistry Chromatography Gel Neuraminic Acids Multiple Myeloma Peptides Glycoprotein Bence Jones Protein |
| Zdroj: | Archives of Biochemistry and Biophysics. 127:725-740 |
| ISSN: | 0003-9861 |
| DOI: | 10.1016/0003-9861(68)90283-x |
| Popis: | Carbohydrate moieties were found to be linked to two human L type Bence-Jones proteins (Hul and Nev) but not to the corresponding light chain from the Nev myeloma protein. The major emphasis was placed upon the characterization of the Hul protein, which consisted of two electrophoretic components. The principal component, accounting for 80% of the total, was identical with the minor component in amino acid composition, but the carbohydrate moieties of the two components differed by at least three residues of glucosamine. The contributions of the oligosaccharide in the principal component were strongly reflected in the analyses of the mixture, which contained an average of four residues of mannose, one residue of galactose, and two residues each of glucosamine, galactosamine, glycolyl neuraminic acid, and fucose. In both the Hul and Nev proteins the oligosaccharides were bound to sites in the variable halves of the molecules. These sites were represented by the following four glycopeptides, derived from homologous segments of the two proteins: Hul Gln-Gln-Glu-Asp-Glu(Ala.Thr)Tyr Hul Gln-Glu-Asp-Glu(Ala, Thr)Tyr-Tyr Nev Ser-Glu-Asp-Glu-Ala-Asp-Tyr Nev Ser-Glu-Asp-Glu-Ala-Asp-Tyr-Tyr The nature of the glycoprotein linkages remains to be elucidated. Peptides accounting for most of the remaining segments of the Hul protein were also isolated and compared with those from the nev and other L type proteins. in the relatively “invariant” carboxyl halves of the proteins, the Hul and Nev proteins differed by the interchange of arginine and lysine residues at position 194, which is associated with the antigenic character Oz. As expected, the substitutions were much more extensive in the amino halves. Finally, the compositions and sequences of segments of both K and L type light chains were examined in an attempt to identify regions with properties similar to those that might be found in the antibody-combining sites of functional γ-globulins. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|