Abstract
The vitelline envelopes of European sea bass and gilthead sea bream are both composed of mainly four proteins with the molecular masses of 90, 52, 48, 45 kDa and 75, 50, 48, 44 kDa, respectively. Each protein has an amino acid composition that is characterized by a high content of proline and glutamic acid and a low content of cysteine, similar to the whole vitelline envelope of both species. The amino acid composition suggests that each protein is distinct but related to the other vitelline envelope proteins. The use of homologous antisera shows that both species have vitelline envelope proteins that are induced by estradiol-17 beta. As males of both species synthesize these proteins after treatment with estradiol-17 beta, the origin is not restricted to the ovaries. Vitellogenin of both European sea bass and gilthead sea bream has the apparent molecular mass of 170 kDa.
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