A redox active site containing murrel cytosolic thioredoxin: Analysis of immunological properties

In this study, we have reported the immunological properties of cDNA encoding thioredoxin which is obtained from the database of Channa striatus (named as CsTRx) cDNA library. The analysis showed that the CsTRx polypeptide contains a thioredoxin domain between Val2 and Asn106. The domain possessed a...

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Veröffentlicht in:Fish & shellfish immunology 2014-01, Vol.36 (1), p.141-150
Hauptverfasser: Palanisamy, Rajesh, Bhatt, Prasanth, Kumaresan, Venkatesh, Chaurasia, Mukesh Kumar, Gnanam, Annie J., Pasupuleti, Mukesh, Kasi, Marimuthu, Arockiaraj, Jesu
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Sprache:eng
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Zusammenfassung:In this study, we have reported the immunological properties of cDNA encoding thioredoxin which is obtained from the database of Channa striatus (named as CsTRx) cDNA library. The analysis showed that the CsTRx polypeptide contains a thioredoxin domain between Val2 and Asn106. The domain possessed a thioredoxin active family at 24–42 along with a redox active site (also known as catalytic center) at 31WCGPC35. The analysis showed that the catalytic center is responsible for the control of protein function. Phylogenetic study showed that CsTRx clustered together with vertebrate TRx-1. Based on the phylogenetic analysis and other bioinformatics analysis, it is confirmed that the characterized CsTRx belongs to TRx-1 family. In addition, the sub-cellular localization prediction analysis showed that CsTRx is a cytosol thioredoxin. The highest gene expression was observed in gill (P 
ISSN:1050-4648
1095-9947
DOI:10.1016/j.fsi.2013.10.016