Published 2007

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Publication details

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

Publisher : Elsevier

International Standard Numbers :
Printed : 1532-0456
Electronic : 1878-1659

Publication type : Academic article

Contributors : Myrnes, Bjørnar; Nilsen, Inge Waller

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Kjetil Aune
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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