Fish eggs are surrounded by a resistant acellular coat commonly called the chorion or zona radiata. This study characterizes the eggshell proteinaceous content of unfertilized eggs of the sea bass Dicentrarchus labrax, with a view to the preparation of immunogens. Solubilization of the purified eggshells was achieved in 8 M urea followed by one- and two-dimensional gel electrophoresis. Glycoproteins were detected using concanavalin-A in one and two-dimensional gels, and the principal glycoproteins had a molecular weight of 47 kDa and 170 kDa. Partial purification of a few polypeptides in the 45 kDa to 55 kDa range was achieved by gel filtration chromatography. Although whole eggshells were relatively insoluble even in 8 M urea, partial purification of these polypeptides enable them to dissolve completely in solutions at low ionic strength. (C) 1994 Wiley-Liss, Inc.

CHARACTERIZATION OF THE MAIN EGG ENVELOPE PROTEINS OF THE SEA BASS DICENTRARCHUS-LABRAX L (TELEOSTEA, SERRANIDAE) / Scapigliati, G; Carcupino, Marcella; Taddei, Ar; Mazzini, M.. - In: MOLECULAR REPRODUCTION AND DEVELOPMENT. - ISSN 1040-452X. - 38:1(1994), pp. 48-53. [10.1002/mrd.1080380109]

CHARACTERIZATION OF THE MAIN EGG ENVELOPE PROTEINS OF THE SEA BASS DICENTRARCHUS-LABRAX L (TELEOSTEA, SERRANIDAE)

CARCUPINO, Marcella;
1994

Abstract

Fish eggs are surrounded by a resistant acellular coat commonly called the chorion or zona radiata. This study characterizes the eggshell proteinaceous content of unfertilized eggs of the sea bass Dicentrarchus labrax, with a view to the preparation of immunogens. Solubilization of the purified eggshells was achieved in 8 M urea followed by one- and two-dimensional gel electrophoresis. Glycoproteins were detected using concanavalin-A in one and two-dimensional gels, and the principal glycoproteins had a molecular weight of 47 kDa and 170 kDa. Partial purification of a few polypeptides in the 45 kDa to 55 kDa range was achieved by gel filtration chromatography. Although whole eggshells were relatively insoluble even in 8 M urea, partial purification of these polypeptides enable them to dissolve completely in solutions at low ionic strength. (C) 1994 Wiley-Liss, Inc.
CHARACTERIZATION OF THE MAIN EGG ENVELOPE PROTEINS OF THE SEA BASS DICENTRARCHUS-LABRAX L (TELEOSTEA, SERRANIDAE) / Scapigliati, G; Carcupino, Marcella; Taddei, Ar; Mazzini, M.. - In: MOLECULAR REPRODUCTION AND DEVELOPMENT. - ISSN 1040-452X. - 38:1(1994), pp. 48-53. [10.1002/mrd.1080380109]
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11388/82341
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