title: Each otoconia polymorph has a protein unique to that polymorph.
abstract: 1. Otoconia, contained within the vestibular portion of the inner ear, are mineralized by one of three polymorphs of calcium carbonate. Each otoconial polymorph contains a unique, major protein. 2. The major protein of calcitic otoconia of members of different vertebrate classes, Amphibia (African clawed frog) and Mammalia (rat), have similar molecular weights. 3. The major protein of calcitic rat otoconia and of vateritic otoconia of the gar may be calcium binding proteins. No protein from the other polymorph, aragonite, appear to have this characteristic.
authors.affiliation: Department of Biology, University of Virginia, Charlottesville 22901.
authors.forename: K G
authors.initials: KG
authors.lastname: Pote
authors.forename: M D
authors.initials: MD
authors.lastname: Ross
mesh_terms: D000558:Ambystoma mexicanum; D000818:Animals; D002119:Calcium Carbonate / Q000378:metabolism*; D002135:Calcium-Binding Proteins / Q000378:metabolism; D008297:Male; D008855:Microscopy, Electron, Scanning; D008970:Molecular Weight; D009673:Notophthalmus viridescens; D010037:Otolithic Membrane / Q000378:metabolism* / Q000648:ultrastructure; D011110:Polymorphism, Genetic; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D011894:Rana pipiens; D051381:Rats; D011919:Rats, Inbred Strains; D012487:Salmonidae; D013045:Species Specificity; D014982:Xenopus laevis
chemical_list: D002135:Calcium-Binding Proteins; D011506:Proteins; D002119:Calcium Carbonate