Partial characterization of natural and recombinant human soluble CD23.
- Rose K Département de Biochimie Médicale, Centre Médical Universitaire, Geneva, Switzerland.
- Turcatti G
- Graber P
- Pochon S
- Regamey PO
- Jansen KU
- Magnenat E
- Aubonney N
- Bonnefoy JY
- 1992-09-15
Published in:
- The Biochemical journal. - 1992
Amino Acid Sequence
Chromatography, High Pressure Liquid
Disulfides
Electrophoresis, Polyacrylamide Gel
Humans
Immunoglobulin E
Mass Spectrometry
Molecular Sequence Data
Peptide Mapping
Receptors, IgE
Recombinant Proteins
Trypsin
English
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.
- Language
-
- English
- Open access status
- green
- Identifiers
-
- DOI 10.1042/bj2860819
- PMID 1417742
- Persistent URL
- https://sonar.ch/global/documents/1411
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