Back to Search
Start Over
Amino acid sequence, post-translational modifications, binding and labelling of porcine odorant-binding protein
- Source :
- Scopus-Elsevier
- Publication Year :
- 1999
-
Abstract
- An odorant-binding protein, migrating in SDS-PAGE with an apparent molecular weight of 22 kDa and an isoelectric point of 4.2, has been purified from pig nasal mucosa. Its complete amino acid sequence was determined by a combination of mass spectrometry and Edman degradation procedures. The protein consists of a single polypeptide chain of 157 amino acids, presenting at the N-terminus a pyroglutamic acid residue. The two cysteine residues, occurring in the primary structure at positions 63 and 155, are involved in an intramolecular disulphide bridge. Sequence comparison with other lipocalins revealed a good similarity with bovine odorant-binding protein, the only member of this class which does not contain disulphide bonds and of which the three-dimensional structure recently has been resolved. Nine out of the 1 6 residues lining the binding pocket in bovine OBP are conserved in the porcine protein, suggesting structural similarities in this region of the molecule. The synthesis of a fluorescent photoaffinity labelling agent and of two tin-containing thymol analogues is also described. These compounds together with other ligands were able to bind the protein as revealed by competitive binding experiments.
- Subjects :
- Azides
Physiology
Swine
Molecular Sequence Data
Photoaffinity Labels
Biology
Ligands
Receptors, Odorant
Fluorescence
Behavioral Neuroscience
chemistry.chemical_compound
Residue (chemistry)
Physiology (medical)
Animals
Amino Acid Sequence
Peptide sequence
chemistry.chemical_classification
Anthracenes
Binding Sites
Edman degradation
Sequence Homology, Amino Acid
Binding protein
Protein primary structure
Sensory Systems
Amino acid
Biochemistry
chemistry
Odorants
Pyroglutamic acid
Protein Processing, Post-Translational
Sequence Analysis
Cysteine
Subjects
Details
- ISSN :
- 0379864X
- Volume :
- 23
- Issue :
- 6
- Database :
- OpenAIRE
- Journal :
- Chemical senses
- Accession number :
- edsair.doi.dedup.....2684e888cf0d585ef2c9a61357c1a5be