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An alpha class glutathione S-transferase from pike liver

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Adapted from a report presented at the VI Russian Symposium

“Proteins and Peptides” (June 11–15, 2013)

Abstract

Glutathione S-transferase (GST) was isolated from the Esox lucius liver and purified to the homogenous state by SDS-PAGE and isoelectrofocusing. It was found to be a homodimer with a subunit molecular weight of 25235.36 Da (HPLC-MS/MS data) and pI of about 6.4. Its substrate specificity, thermal stability, some kinetic characteristics, and optimum pH were studied. The enzyme was identified as Alpha class GST.

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Abbreviations

CDNB:

1-chloro-2,4-dinitrobenzene

DCNB:

1,2-dichloro-4-nitrobenzene

EtA:

etacrynic acid

GST:

glutathione S-transferase

4NQ:

4-nitroquinoline N-oxide

tPB:

trans-4-phenyl-3-buten-2-one

tSO:

trans-stilbene oxide

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Correspondence to E. V. Borvinskaya.

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Original Russian Text © E.V. Borvinskaya, L.P. Smirnov, N.N. Nemova, 2013, published in Bioorganicheskaya Khimiya, 2013, Vol. 39, No. 5, pp. 558–564.

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Borvinskaya, E.V., Smirnov, L.P. & Nemova, N.N. An alpha class glutathione S-transferase from pike liver. Russ J Bioorg Chem 39, 498–503 (2013). https://doi.org/10.1134/S1068162013050051

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  • DOI: https://doi.org/10.1134/S1068162013050051

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