Partial characterization of natural and recombinant human soluble CD23
| Autor: | Gerardo Turcatti, N Aubonney, Pierre Graber, P O Regamey, S Pochon, J Y Bonnefoy, Keith Rose, E Magnenat, K U Jansen |
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| Rok vydání: | 1992 |
| Předmět: |
Stereochemistry
Molecular Sequence Data Peptide Mapping Biochemistry Mass Spectrometry law.invention Residue (chemistry) Protein structure law protein purification Protein purification Humans Trypsin Amino Acid Sequence Disulfides protein structure Molecular Biology Peptide sequence Polyacrylamide gel electrophoresis Protein secondary structure Chromatography High Pressure Liquid Edman degradation Receptors IgE Chemistry Cell Biology Immunoglobulin E Recombinant Proteins protein analysis Recombinant DNA cd23 antigen Electrophoresis Polyacrylamide Gel Research Article |
| Zdroj: | Biochemical Journal. 286:819-824 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj2860819 |
| Popis: | The purification to homogeneity of an active soluble 25 kDa fragment of CD23, produced in insect cells using the baculovirus expression system, is described. Peptide mapping and analysis by Edman degradation and mass spectrometry permitted partial characterization of the protein. A total of 165 out of 172 residues, including N-terminal and C-terminal regions, were mapped. The positions of the two disulphide bonds in the IgE-binding region were also determined: residue 110 is joined to residue 124, and residue 42 to residue 133. Natural CD23 25 kDa fragment was also analysed and found to possess the same disulphide bond arrangement. These results extend the previously noted sequence similarity with lectins to elements of secondary structure. |
| Databáze: | OpenAIRE |
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