Publisert 2007

Les på engelsk


Tidsskrift : Comparative Biochemistry and Physiology - Part C: Toxicology & Pharmacology , vol. 144 , p. 403–407 , 2007

Utgiver : Elsevier

Internasjonale standardnummer :
Trykt : 1532-0456
Elektronisk : 1878-1659

Publikasjonstype : Vitenskapelig artikkel

Bidragsytere : Myrnes, Bjørnar; Nilsen, Inge Waller

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Kjetil Aune


Glutathione S-transferase from the digestive gland of the cold-adapted marine bivalve Icelandic scallop was purified to apparent homogeneity by single GSTrap chromatography. The enzyme appeared to be a homodimer with subunit Mr 22,000 having an optimum catalytic activity at pH 6.5–7. Enzymatic analysis of scallop GST using the substrates 1-chloro-2,4-dinitrobenzene (CDNB) and glutathione resulted in apparent values for Km GST and Km CDNB of 0.3 mM and 0.4 mM, respectively. The scallop GST lost activity faster than porcine GST when exposed to increased temperatures, but both enzymes needed 10 min incubation at 60 °C for complete inactivation. A partial coding sequence was identified in cDNA synthesised from digestive gland mRNA. Comparison to known sequences indicates that the gene product is a glutathione S-transferase, and the predicted Icelandic scallop GST protein scores