Title: | "Pheromaxein, the pheromonal steroid-binding protein, is a major protein synthesized in porcine submaxillary salivary glands" |
Address: | "AFRC Institute of Animal Physiology and Genetics Research, Cambridge Research Station, Babraham Hall" |
ISSN/ISBN: | 0022-0795 (Print) 0022-0795 (Linking) |
Abstract: | "Submaxillary salivary gland tissue from large White, Gottingen miniature and Meishan (Chinese) breeds of pig, and European wild boars, was incubated with [35S]methionine. The radiolabelled amino acid was incorporated into protein in all incubations as demonstrated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). Specifically [35S]methionine was predominantly incorporated into the alpha- and beta-charge isomers of pheromaxein, a 16-androstene steroid-binding protein, as shown by SDS-PAGE in combination with vertical isoelectric focusing on polyacrylamide slab gels. The synthesis of pheromaxein occurred in submaxillary gland tissue from both sexes, including tissues stored frozen at -70 degrees C for long periods. There was little evidence for pheromaxein synthesis in parotid gland tissue or skeletal muscle. Total protein, pheromaxein and total 16-androstenes were determined in the submaxillary gland cytosols of six mature Gottingen miniature boars and a positive correlation was found between these glandular constituents. The amounts of endogenous pheromaxein relative to total protein in the submaxillary gland cytosols (range 10.3-18.0%), together with the predominant synthesis of this protein in vitro, indicate that pheromaxein is a major protein produced in porcine submaxillary glands, particularly in those of the male" |
Keywords: | "Androstenes/metabolism Animals Carrier Proteins/*biosynthesis Cytosol/metabolism Female Intercellular Signaling Peptides and Proteins Male Pheromones/*biosynthesis Proteins/metabolism Submandibular Gland/*metabolism Swine/*metabolism Swine, Miniature/meta;" |
Notes: | "MedlineBooth, W D von Glos, K I eng England 1991/02/01 J Endocrinol. 1991 Feb; 128(2):205-12. doi: 10.1677/joe.0.1280205" |