Characterization of a recombinant mu-class glutathione S-transferase fromTaenia solium
✍ Scribed by N. Vibanco-Pérez; L. Jiménez; G. Mendoza-Hernández; A. Landa
- Publisher
- Springer-Verlag
- Year
- 2002
- Tongue
- English
- Weight
- 185 KB
- Volume
- 88
- Category
- Article
- ISSN
- 1432-1955
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## Abstract Glutathione __S__‐transferases (GSTs) are a family of detoxifying enzymes that catalyze the conjugation of glutathione (GSH) to electrophiles, thereby increasing the solubility of GSH and aiding its excretion from the cell. In this study, a glutatione __S__‐transferase from the gills of
## Abstract Glutathione __S__‐transferases (GSTs) are a family of detoxifying enzymes that catalyze the conjugation of glutathione (GSH) to electrophiles, thereby increasing the solubility of xenobiotics and aiding its excretion from the cell. The present work presents the inhibition of a mu‐class
## Abstract A cDNA clone coding for a mu‐class glutathione __S__‐transferase (GST) was isolated from a hepatopancreas cDNA library from the shrimp __Litopenaeus vannamei__. The deduced amino acid sequence (215 amino acids) has >50% identity to rodents and other mammals mu‐class GSTs. Using RT‐PCR,