FN Archimer Export Format
PT J
TI Crassostrea gigas ferritin: cDNA sequence analysis for two heavy chain type subunits and protein purification
BT 
AF DURAND, Jean-Pierre
   GOUDARD, Françoise
   PIERI, Jacques
   ESCOUBAS, Jean-Michel
   SCHREIBER, Nathalie
   CADORET, Jean-Paul
AS 1:;2:;3:;4:;5:;6:;
FF 1:;2:;3:;4:;5:PDG-DRV-VP-PBA;6:PDG-DRV-VP-PBA;
C1 Univ Nantes, Lab Biochim & Radiobiochim, GERMETRAD, SMAB,UPRES,EA 2160, F-44322 Nantes 3, France.
   Univ Montpellier 2, CNRS, Def & Resistance Invertebres Marins, IFREMER,UMII, F-34095 Montpellier, France.
   IFREMER, Prod & Biotechnol Algues, F-44311 Nantes, France.
C2 UNIV NANTES, FRANCE
   UNIV MONTPELLIER 2, FRANCE
   IFREMER, FRANCE
SI MONTPELLIER
   NANTES
SE PDG-DRV-RA-GPIA
   PDG-DRV-VP-PBA
IN WOS Ifremer jusqu'en 2018
   copubli-univ-france
IF 2.705
TC 55
UR https://archimer.ifremer.fr/doc/2004/publication-693.pdf
LA English
DT Article
DE ;Iron;IRE;EST;Oyster
AB Ferritin has been shown as being the principal iron storage in the majority of living organisms. In marine species, ferritin is also involved in high-level accumulation of Po-210. As part of our work on the investigation of these radionuclides' concentration in natural environment, ferritin was searched at the gene and protein level. Ferritin was purified from the visceral mass of the oyster Crassostrea gigas by ion-exchange chromatography and HPLC. SDS-PAGE revealed one band of 20 kDa. An Expressed Sequence Tag (EST) library was screened and led to the identification of two complementary DNA (cDNA) involved in ferritin subunit expression. The complete coding sequences and the untranslated regions (UTRs) of the two genes were obtained and a 5' Rapid Amplification of cDNA Ends (RACE) was used to obtain the two iron-responsive elements (IREs) with the predicted stem-loop structures usually present in the 5'-UTR of ferritin mRNA. Sequence alignment in amino acid of the two new cDNA showed an identity with Pinctada fucata (85.4-88.3%), Lymnaea stagnalis (79.3-82.2%) and Helix pomatia (79.1-79.1%). The residues responsible for the ferroxidase center, conserved in all vertebrate H-ferritins, are present in the two oyster ferritin subunits. Oyster ferritins do not present the special characteristics of other invertebrate ferritins like insect ferritins but have some functional similarities with the vertebrate H chains ferritin. 
PY 2004
PD SEP
SO Gene
SN 0378-1119
PU Elsevier
VL 338
IS 2
UT 000223777400005
BP 187
EP 195
DI 10.1016/j.gene.2004.04.027
ID 693
ER

EF