D. Sellos et al., MOLECULAR-CLONING OF HEMOCYANIN CDNA FROM PENAEUS-VANNAMEI (CRUSTACEA, DECAPODA) - STRUCTURE, EVOLUTION AND PHYSIOLOGICAL-ASPECTS, FEBS letters, 407(2), 1997, pp. 153-158
Hemocyanin is present as 2 subunits in the hemolymph of Penaeus vannam
ei. Isolated from a hepatopancreas cDNA Library of this penaeid shrimp
, the cDNA chain (2095 bp) corresponds to a full length hemocyanin mes
senger as determined by Northern hybridization, with a short 5' untran
slated region (17 bp), an open reading frame (1989 bp counting initiat
ion and termination codons) coding for a signal peptide (13 residues)
and a mature hemocyanin (648 amino acids), and a 3' untranslated regio
n (89 bp) followed by the polyadenylated track, It is the first time t
hat the existence of a hydrophobic signal peptide is shown in arthropo
d hemocyanin. Two primary N-terminal sequences are determined and a 3-
fold increase of mRNA content, measured in the hepatopancreas during t
he premoult stages, is reported, The low level of polymorphism shown b
y P. vannamei hemocyanin, along with its weak percentage identity with
counterparts and its similarity with hemocyanin from Panulirus interr
uptus, suggests that this arthropod hemocyanin may be a primitive subu
nit that has evolved independently, following gene duplication. (C) 19
97 Federation of European Biochemical Societies.