Abstract

Molecular characterization of thioredoxin-1 and thioredoxin reductase activity in mud crab Scylla paramamosain

Author(s): J.H. Hu1,2*, F.Y. Zhang1*, K.J. Jiang1, Y.B. Fang1,2, J. Wang1,2, M. Zhao1,2, Z.G. Qiao1 and L.B. Ma1

The thioredoxin (Trx) system consists of thioredoxin reductase (TrxR), Trx, and nicotinamide adenine dinucleotide phosphate (NADPH). TrxR is an NADPH-dependent oxidoreductase. Trx is a ubiquitous small protein with a redox-active disulfide bridge that plays important regulatory roles in some vital metabolic reactions. In this study, a cDNA sequence (SpTrx1) showing high identity to the first Trx gene was isolated from a hepatopancreas cDNA library of the mud crab Scylla paramamosain. The full-length cDNA of SpTrx1 consisted of 672 bp and contained a complete open reading frame of 318 bp encoding a polypeptide of 105 amino acids.

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