Skip to main content

Purification and characterization of pheromaxein, the porcine steroid-binding protein. A member of the secretoglobin superfamily

Austin, Corrine J., Emberson, Louise M., Nicholls, Peter J. (2004) Purification and characterization of pheromaxein, the porcine steroid-binding protein. A member of the secretoglobin superfamily. European Journal of Biochemistry, 271 (13). pp. 2593-2606. ISSN 0014-2956. (doi:10.1111/j.1432-1033.2004.04188.x) (Access to this publication is currently restricted. You may be able to access a copy if URLs are provided) (KAR id:57)

Language: English

Restricted to Repository staff only
[thumbnail of Austin_et_al_2004_Eur_J_Biochem_PJN.pdf]
Official URL:


Low molecular mass proteins are implicated in chemical communication throughout mammalian species, being involved in both perception and delivery of pheromonal compounds. In boars, pheromones are secreted in saliva to cause oestrous sows to take up the mating stance. These pheromones are the 16-androstene steroids, 5alpha-androsten-3alpha-ol and 5alpha-androsten-3-one. The submaxillary glands of boars contain a low molecular mass protein, pheromaxein, which is capable of binding these 16-androstene pheromones. Pheromaxein was purified, cloned and characterized. It was found to be a nonglycosylated heterodimeric protein, belonging to the secretoglobin superfamily and the major 16-androstene-binding protein present in submaxillary salivary glands of the boar. One subunit, pheromaxein A, was found to be homologous to prostatein peptides, C1 and C2 and lipophilin A and B, whereas the other subunit, pheromaxein C, was homologous to prostatein peptide C3 and lipophilin C. Transcription of pheromaxein A was limited to the prostate and submaxillary salivary glands from both the boar and sow, whereas transcription of the other subunit, pheromaxein C, was more widespread. This is similar to the transcription distribution of lipophilin in humans. Many isoforms of pheromaxein were found to exist, with a molecular mass range of 17,415-18,159 Da; these are probably products of a multigene family. Post-translational modifications, to generate mature pheromaxein isoforms, probably include C-terminal cleavage of pheromaxein A, followed by additional modifications.

Item Type: Article
DOI/Identification number: 10.1111/j.1432-1033.2004.04188.x
Uncontrolled keywords: androstenone; lipocalin; pheromaxein; secretoglobin; steroid-binding protein
Subjects: Q Science
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Susan Davies
Date Deposited: 19 Dec 2007 17:51 UTC
Last Modified: 16 Nov 2021 09:38 UTC
Resource URI: (The current URI for this page, for reference purposes)
  • Depositors only (login required):

Total unique views for this document in KAR since July 2020. For more details click on the image.