A Mu-class glutathione S-transferase from gills of the marine shrimp Litopenaeus vannamei: purification and characterization.

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Contreras-Vergara CA, Valenzuela-Soto E, Garcia-Orozco KD, Sotelo-Mundo RR, Yepiz-Plascencia G

A Mu-class glutathione S-transferase from gills of the marine shrimp Litopenaeus vannamei: purification and characterization.

J Biochem Mol Toxicol. 2007;21(2):62-7.

PubMed ID

17427177 [ View in PubMed

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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 the marine shrimp Litopenaeus vannamei was purified by affinity chromatography using a glutathione-agarose affinity column. GST was purified to homogeneity as judged by reducing SDS-PAGE and zymograms. This enzyme is a homodimer composed of approximately 25-kDa subunits and identified as a Mu-class GST based on its activity against 1-chloro-2,4-dinitrobenzene (CDNB) and internal peptide sequence. The specific activity of purified GST was 440.12 micromol/(min mg), and the K(m) values for CDNB and GSH are very similar (390 and 335 microM, respectively). The intersecting pattern of the initial velocities of this enzyme in the Lineweaver-Burke plot is consistent with a sequential steady-state kinetic mechanism. The high specific activity of shrimp GST may be related to a highly effective detoxification mechanism necessary in gills since they are exposed to the external and frequently contaminated environment.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Glutathione	Glutathione S-transferase Mu 1	Protein	Humans	Unknown	Not Available	Details