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Structure of arthropod hemocyanin
Author(s) -
Bak Henk J.,
Neuteboom Ben,
Jekel Peter A.,
Soeter Nell M.,
Vereijken Johan M.,
Beintema Jaap J.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81402-8
Subject(s) - hemocyanin , arthropod , crustacean , biology , invertebrate , protein subunit , peptide sequence , ecology , zoology , biochemistry , gene , genetics , antigen
Hemocyanins are large multi‐subunit copper proteins that transport oxygen in many arthropods and molluscs. The amino acid sequence of subunit a of Panulirus interruptus hemocyanin (657 residues) has been completed and fitted to the electron‐density map (3.2 Å resolution). Comparison of amino acid sequence data for several different hemocyanin subunits of arthropod species indicated that the general features of the polypeptide architecture as found in spiny lobster hemocyanin occur in all arthropods. This structure must therefore be at least as old as the estimated time of divergence of crustaceans and chelicerates, 540–600 million years ago.