New Zealand Journal of Marine and Freshwater Research abstracts
Characterisation of cavortin, the major haemolymph protein of the Pacific oyster
(Crassostrea gigas)
Paul D. Scotti
Sally C. Dearing
David R. Greenwood
The Horticulture and Food Research Institute of New Zealand Ltd
Mt. Albert Research Centre
Private Bag 92 169
Auckland, New Zealand
email: dgreenwood@hortresearch.co.nz
Abstract Evidence suggests that members of the oyster genus Crassostrea share
a common haemolymph protein. Cavortin, the major haemolymph protein of the
Pacific oyster (Crassostrea gigas), comprises 174 amino acid residues
totalling 19.4 kDa and is rich in histidine and aspartic acid. The protein
consists of a single Cu/Zn SOD (superoxide dismutase) derived domain showing
homology to each of the three SOD-like domains of pernin, the related 60 kDa
protein from the green-lipped mussel (Perna canaliculus). Despite some
homology to Cu/Zn SOD sequences we found no compelling evidence that it has
retained SOD function. Cavortin has affinity for several divalent cations,
particularly iron. Each cavortin monomer is able to bind 8–11 iron ions,
but can sequester considerably more iron, presumably by forming spheroid particles.
The primary function of cavortin, like pernin, has been altered during the
course of evolution, but has yet to be determined unambiguously. A likely role
is as a metal ion chaperone.
Keywords oyster; Crassostrea gigas;haemolymph protein;
cavortin; pernin; metal ions
New Zealand Journal of Marine and Freshwater Research, 2007, Vol. 41:
91–101
0028–8330/07/4101–0091 © The Royal Society
of New Zealand 2007
M06057; Online publication date 9 March 2007. Received 5 September
2006; accepted 13 January 2007
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