Title : Structural analysis and localization of the carbohydrate moieties of a soluble human
interferon gamma receptor produced in baculovirus-infected insect cells
Abstract :
- A soluble form of the human interferon gamma receptor that is required for the identification of interferon gamma antagonists was expressed in baculovirus-infected insect cells
- The protein carried N-linked carbohydrate and showed a heterogeneity on denaturing polyacrylamide gels
- We investigated the utilization of the potential sites for N-linked glycosylation and the structure of the carbohydrate moieties of this soluble receptor
- Amino acid sequence analysis and ion spray mass spectrometry revealed that of the five potential sites for N-linked glycosylation, Asn17 and Asn69 were always utilized, whereas Asn62 and Asn162 were utilized in approximately one-third of the protein population
- Asn223 was never found to be glycosylated
- The soluble receptor was treated with N-glycosidase F and the oligosaccharides released were analyzed by matrix-assisted laser desorption mass spectrometry, which showed that the protein carried six types of short carbohydrate chains
- The predominant species was a hexasaccharide of molecular mass 1,039 , containing a fucose subunit linked to the proximal N-acetylglucosamine residue: [formula: see text
Output (sent_index, trigger,
protein,
sugar,
site):
- 0. receptor, , interferon gamma receptor, the carbohydrate moieties, -
- 2. carried, , protein, N-linked carbohydrate, -
- 3. receptor, , receptor, the carbohydrate moieties, -
- 4. utilized, , -, -, Asn17 and Asn69
- 4. utilized, , -, -, Asn62 and Asn162
- 5. glycosylated, , -, -, Asn223
- 7. mass, , mass 1,039, a hexasaccharide, -
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):
- 4. interferon gamma receptor, -, Asn17 and Asn69
- 4. interferon gamma receptor, -, Asn62 and Asn162
- 5. interferon gamma receptor, -, Asn223