Document Detail


Subtypes of odorant-binding proteins--heterologous expression and ligand binding.
MedLine Citation:
PMID:  9660186     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Odorant-binding proteins (OBP) in the mucus of the olfactory epithelium are thought to transfer the hydrophobic odorous compounds through the aqueous barrier towards the chemo-sensory cells. To evaluate their binding properties, two distinct OBP subtypes of the rat were expressed as N-terminal His-tagged fusion proteins in Escherichia coli, thus allowing an efficient purification. Based on gel chromatography and CD spectroscopy analysis the recombinant OBP subtypes seem to share several structural features with other members of the lipocalin family. Approaches to elucidate whether heterologous expressed OBPs interact with odorous compounds revealed that OBP1 specifically binds 2-[3H]-isobutyl-3-methoxypyrazine whereas OBP2 did not shown any specific binding to this compound. In contrast, the chromophore 1-anilinonaphthalene 8-sulfonic acid (1,8-ANS) specifically interacted with OBP2 but not with OBP1. Displacement experiments monitored by the relative fluorescence intensity revealed that fatty acids with appropriate chain length act as efficient competitors. Some odorous compounds, notably lilial (p-tert-butyl-alpha-methyl dihydrocinnamic aldehyde) and citralva (3,7-dimethyl-2,6-octadienenitrile), also displaced efficiently the chromophore, whereas pyrazine derivatives including 2-isobutyl-3-methoxypyrazine and other odorants did not. These results indicate that rat OBPs have distinct ligand specificities.
Authors:
D Löbel; S Marchese; J Krieger; P Pelosi; H Breer
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  254     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1998 Jun 
Date Detail:
Created Date:  1998-07-21     Completed Date:  1998-07-21     Revised Date:  2007-07-23    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  318-24     Citation Subset:  IM    
Affiliation:
University of Stuttgart-Hohenheim, Institute of Physiology, Stuttgart, Germany.
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MeSH Terms
Descriptor/Qualifier:
Anilino Naphthalenesulfonates
Animals
Binding, Competitive
Circular Dichroism
Fatty Acids / metabolism
Fluorescent Dyes
Gene Expression
Ligands
Odors
Olfactory Mucosa / metabolism
Protein Structure, Secondary
Rats
Receptors, Odorant / classification*,  genetics*,  metabolism
Recombinant Proteins / classification,  genetics,  metabolism
Chemical
Reg. No./Substance:
0/Anilino Naphthalenesulfonates; 0/Fatty Acids; 0/Fluorescent Dyes; 0/Ligands; 0/Receptors, Odorant; 0/Recombinant Proteins; 0/odorant-binding protein; 82-76-8/1-anilino-8-naphthalenesulfonate

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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