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Identification and characterization of the major components of the Oncorhynchus mykiss Egg Chorion
Author(s) -
Brivio Maurizio F.,
Bassi Rosaria,
Cotelli Franco
Publication year - 1991
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/mrd.1080280114
Subject(s) - biology , glycoprotein , concanavalin a , biochemistry , oviduct , molecular mass , extracellular , oncorhynchus , asparagine , fish <actinopterygii> , enzyme , in vitro , fishery , endocrinology
The extracellular coat surrounding the fish egg, commonly called the chorion, is a primary envelope that confers biochemical and morphological identity typical of the species. Purified chorions can be easily isolated from either oocytes or ovulated eggs. The aim of this work was to analyze the macromolecular composition of the various chorion components in Oncorhynchus mykiss (Salmonids). SDS‐PAGE analysis of purified chorion showed a reproducible pattern of four major components (129, 62, 54, and 47 kD), representing about 80% of total chorion proteins. The 129 and 47 kD polypeptides were periodic‐acid Schiff (PAS) and concanavalin A positive. After chemical and enzymatic deglycosylation treatments only the 129 and 47 kD components proved to be glycosylated and to belong to the “asparagine‐linked” glycoprotein family. Furthermore, peptide mapping performed on isolated polypeptides showed comigrating fragments on SDS‐PAGE. These results suggest that the four main chorion polypeptides might share common structural features.