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- W2363348575 abstract "Ferritin is involved in biomineralization of mollusk shells,although the molecular mechanism of this process is not fully understood.High level of recombinant protein rGST-MmeFer in Meretrix meretrix was obtained using Es-cherichia coli and then identified using in-gel digestion and LC-ESI-MS/MS.After rGST-MmeFer was purified on the GST affinity column and then the GST tag was cleaved,the remaining recombinant MmeFer(rMmeFer) exhibited similar func-tion of iron oxidation and uptake in vitro.Rabbit anti-rGST-MmeFer polyclonal antibodies was prepared using the purified rGST-MmeFer and then used in Western blot analysis.The result showed that ferritin was expressed in all tissues of M.meretrix,with the highest expression in the digestive gland and the lowest in the foot.mRNA expression of the M.meretrix ferritin showed the highest expression in the mantle,followed by the digestive gland,and the lowest in the gill.Significant expression variation was found between the tissues(P0.05) .The results laid foundation for the functional analysis of fer-ritin involved in the shell formation of mollusks." @default.
- W2363348575 created "2016-06-24" @default.
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- W2363348575 date "2011-01-01" @default.
- W2363348575 modified "2023-09-25" @default.
- W2363348575 title "CHARACTERIZATION OF RECOMBINANT EXPRESSION AND TISSUE EXPRESSION OF FERRITIN IN CLAM MERETRIX MERETRIX" @default.
- W2363348575 hasPublicationYear "2011" @default.
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