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. Copyright © 1991 Wiley‐Liss, Inc.

Identification and characterization of the major components of the Oncorhynchus mykiss Egg Chorion

BRIVIO, MAURIZIO FRANCESCO;
1991

Abstract

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. Copyright © 1991 Wiley‐Liss, Inc.
Egg envelope; Fish; Glycoproteins; Trout;
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11383/13259
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