Literature DB >> 3337807

Properties of odour-binding glycoproteins from rat olfactory epithelium.

E E Fesenko1, V I Novoselov, M F Bystrova.   

Abstract

The specific membrane glycoproteins with high affinity for camphor and decanal were isolated from rat olfactory epithelium. Antibodies to these glycoproteins inhibited both the electroolfactogram and the binding of odorants. The enzyme immunoassay has shown these glycoproteins to be present in the olfactory epithelium of rat, mouse, guinea-pig and hamster but not in that of frog and carp. The molecular mass of the odour-binding glycoproteins from rat olfactory epithelium solubilized by Triton X-100 was approx. 140 kDa. They consisted of two subunits (88 and 55 kDa). The 88 kDa subunit was capable of binding odorants. The data obtained suggest that the glycoproteins isolated have some properties that make them plausible candidates for olfactory receptor molecules.

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Year:  1988        PMID: 3337807     DOI: 10.1016/0005-2736(88)90259-3

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  3 in total

1.  Molecular mechanisms of odor-sensing.

Authors:  E E Fesenko
Journal:  J Protein Chem       Date:  1989-06

2.  Membrane fluidity changes of liposomes in response to various odorants. Complexity of membrane composition and variety of adsorption sites for odorants.

Authors:  M Kashiwayanagi; A Suenaga; S Enomoto; K Kurihara
Journal:  Biophys J       Date:  1990-10       Impact factor: 4.033

3.  Electro-olfactogram and multiunit olfactory receptor responses to binary and trinary mixtures of amino acids in the channel catfish, Ictalurus punctatus.

Authors:  J Caprio; J Dudek; J J Robinson
Journal:  J Gen Physiol       Date:  1989-02       Impact factor: 4.086

  3 in total

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