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Amino acid sequence, post-translational modifications, binding and labelling of porcine odorant-binding protein

Authors :
Andrea Scaloni
Paolo Pelosi
Angela Amoresano
Elio Napolitano
Sara Paolini
Silvana Marchese
Paolini, S
Scaloni, A
Amoresano, Angela
Marchese, S
Napolitano, E
Pelosi, P.
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.

Details

ISSN :
0379864X
Volume :
23
Issue :
6
Database :
OpenAIRE
Journal :
Chemical senses
Accession number :
edsair.doi.dedup.....2684e888cf0d585ef2c9a61357c1a5be