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Published 2007

Read in Norwegian

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

If you have questions about the publication, you may contact Nofima’s Chief Librarian.

Kjetil Aune
Chief Librarian
kjetil.aune@nofima.no

Summary

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