Molecular cloning of α-2-macroglobulin from hemocytes of common periwinkle Littorina littorea.
Fish Shellfish Immunol
; 39(2): 136-7, 2014 Aug.
Article
em En
| MEDLINE
| ID: mdl-24830774
ABSTRACT
We report the sequence of the proteinase inhibitor with a wide inhibition spectrum, α-2-macroglobulin (α2M), belonging to the thioester superfamily of proteins. This is the first α2M sequence from coenogastropod prosobranch snails. The full-length cDNA was cloned by RACE method, spans 7897 bp and contains an open reading frame of 5460 bp. The ORF encodes a protein of 1819 amino acids. The deduced mature protein contains 1795 amino acids with a molecular weight of 200 kDa and isoelectric point of 5.00. Littorina littorea α2M bears 4 conserved α2M domains and one internal thioester. Phylogenetic analysis showed that the sequence forms well supported cluster with Mollusca species and other representatives of Lophotrochozoa.
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Base de dados:
MEDLINE
Assunto principal:
Filogenia
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Caramujos
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Alfa-Macroglobulinas
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Hemócitos
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Imunidade Inata
Idioma:
En
Ano de publicação:
2014
Tipo de documento:
Article
País de afiliação:
Federação Russa