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Recombinant expression and partial characterization of the human formyl peptide receptor
- Source :
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1178:302-306
- Publication Year :
- 1993
- Publisher :
- Elsevier BV, 1993.
-
Abstract
- FMLP-receptor DNA was expressed in Escherichia coli. The expressed product could specifically bind FMLP. This is the first-reported expression of a functional FMLP receptor in Escherichia coli. We confirm that receptor glycosylation is not essential for ligand binding. A deletion mutant did not bind FMLP, suggesting that the deleted portion plays a role in ligand binding.
- Subjects :
- Models, Molecular
Glycosylation
Molecular Sequence Data
Biology
medicine.disease_cause
law.invention
chemistry.chemical_compound
law
Escherichia coli
medicine
Humans
Amino Acid Sequence
Receptors, Immunologic
Receptor
Molecular Biology
Peptide sequence
Mutation
Formyl peptide receptor
Base Sequence
hemic and immune systems
Chemotaxis
Cell Biology
Receptors, Formyl Peptide
Recombinant Proteins
Biochemistry
chemistry
Recombinant DNA
lipids (amino acids, peptides, and proteins)
Subjects
Details
- ISSN :
- 01674889
- Volume :
- 1178
- Database :
- OpenAIRE
- Journal :
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Accession number :
- edsair.doi.dedup.....75e9194a3753f25c0e650abb1b372a09
- Full Text :
- https://doi.org/10.1016/0167-4889(93)90208-7