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Characterization of porcine Alpha-class glutathione transferase A1-1
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för neurokemi.ORCID-id: 0000-0002-6416-064X
2011 (Engelska)Ingår i: Archives of Biochemistry and Biophysics, ISSN 0003-9861, E-ISSN 1096-0384, Vol. 507, nr 2, s. 205-211Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

An Alpha-class glutathione transferase (GST) has been cloned from pig gonads. In addition to two conservative point mutations our nucleotide sequence presents a frame shift resulting from a missing A as compared to a previously published porcine GST A1-1 sequence. The deduced C-terminal amino-acid segment of the protein differs between the two variants. Repeated sequencing of cDNA isolated from different tissues and animals ruled out the possibility of a cloning artifact, and the deduced amino acid sequence of our clone showed higher similarity to related mammalian GST sequences. Hereafter, we refer to our cloned enzyme as GST A1-1 and to the previously published enzyme as GST A1-1(∗). The study of the tissue distribution of the GSTA1 mRNA revealed high expression levels in many organs, in particular adipose tissue, liver, and pituitary gland. Porcine GST A1-1 was expressed in Escherichia coli and its kinetic properties were determined using alternative substrates. The catalytic activity in steroid isomerization reactions was at least 10-fold lower than the corresponding values for porcine GST A2-2, whereas the activity with 1-chloro-2,4-dinitrobenzene was approximately 8-fold higher. Differences in the H-site residues of mammalian Alpha-class GSTs may explain the catalytic divergence.

Ort, förlag, år, upplaga, sidor
2011. Vol. 507, nr 2, s. 205-211
Nyckelord [en]
Sus scrofa, Glutathione transferase A1-1, Alternative sequence, Substrate selectivity
Nationell ämneskategori
Kemi
Forskningsämne
neurokemi med molekylär neurobiologi
Identifikatorer
URN: urn:nbn:se:su:diva-53692DOI: 10.1016/j.abb.2010.12.015ISI: 000288058000001PubMedID: 21172301OAI: oai:DiVA.org:su-53692DiVA, id: diva2:391146
Tillgänglig från: 2011-01-24 Skapad: 2011-01-24 Senast uppdaterad: 2017-12-11Bibliografiskt granskad

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Mannervik, Bengt
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Institutionen för neurokemi
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Archives of Biochemistry and Biophysics
Kemi

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