Abstract:
:Hemocyanin is present as 2 subunits in the hemolymph of Penaeus vannamei. Isolated from a hepatopancreas cDNA library of this penaeid shrimp, the cDNA chain (2095 bp) corresponds to a full length hemocyanin messenger as determined by Northern hybridization, with a short 5' untranslated region (17 bp), an open reading frame (1989 bp counting initiation and termination codons) coding for a signal peptide (13 residues) and a mature hemocyanin (648 amino acids), and a 3' untranslated region (89 bp) followed by the polyadenylated track. It is the first time that the existence of a hydrophobic signal peptide is shown in arthropod hemocyanin. Two primary N-terminal sequences are determined and a 3-fold increase of mRNA content, measured in the hepatopancreas during the premoult stages, is reported. The low level of polymorphism shown by P. vannamei hemocyanin, along with its weak percentage identity with counterparts and its similarity with hemocyanin from Panulirus interruptus, suggests that this arthropod hemocyanin may be a primitive subunit that has evolved independently, following gene duplication.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Sellos D,Lemoine S,Van Wormhoudt Adoi
10.1016/s0014-5793(97)00350-5subject
Has Abstractpub_date
1997-04-28 00:00:00pages
153-8issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(97)00350-5journal_volume
407pub_type
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