Ligand Binding Properties of Odorant-Binding Protein OBP5 from
affinity
circular dichroism
fluorescent assay
isothermal microcalorimetry
lipocalin
odorant
odorant-binding protein
purification
Journal
Biology
ISSN: 2079-7737
Titre abrégé: Biology (Basel)
Pays: Switzerland
ID NLM: 101587988
Informations de publication
Date de publication:
20 Dec 2022
20 Dec 2022
Historique:
received:
14
11
2022
revised:
07
12
2022
accepted:
13
12
2022
entrez:
21
1
2023
pubmed:
22
1
2023
medline:
22
1
2023
Statut:
epublish
Résumé
Odorant-binding proteins (OBPs) are abundant soluble proteins secreted in the nasal mucus of a variety of species that are believed to be involved in the transport of odorants toward olfactory receptors. In this study, we report the functional characterization of mouse OBP5 (mOBP5). mOBP5 was recombinantly expressed as a hexahistidine-tagged protein in bacteria and purified using metal affinity chromatography. The oligomeric state and secondary structure composition of mOBP5 were investigated using gel filtration and circular dichroism spectroscopy. Fluorescent experiments revealed that mOBP5 interacts with the fluorescent probe
Identifiants
pubmed: 36671695
pii: biology12010002
doi: 10.3390/biology12010002
pmc: PMC9855133
pii:
doi:
Types de publication
Journal Article
Langues
eng
Subventions
Organisme : Agence Nationale de la Recherche:
ID : ANR-18-CE42-0012
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