parB: an auxin-regulated gene encoding glutathione S-transferase.
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چکیده
منابع مشابه
parB: an auxin-regulated gene encoding glutathione S-transferase.
We have isolated an auxin-regulated cDNA, parB, from the early stage of cultured tobacco mesophyll protoplasts. The expression of parB was observed during transition from G0 to the S phase of tobacco mesophyll protoplasts cultured in vitro. The predicted amino acid sequence of parB cDNA has 213 amino acid residues with a relative molecular weight of 23,965. Nucleotide sequence analysis revealed...
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AIM Helicobacter pylori infection, though common, leads to gastric cancer (GC) in less than 1% individuals, suggesting the role of host factors. We previously reported the role of glutathione-S-transferase (GST) polymorphisms, the gene encoding a carcinogen-detoxifying enzyme, in GC. This study was aimed to evaluate GST enzyme activity, GST polymorphism, glutathione (GSH) levels and H. pylori i...
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Nasopharyngeal carcinoma (NPC) is a serious health problem in Thailand. It is caused by the combined effects of Epstein-Barr virus (EBV), carcinogens and genetic susceptibility. The glutathione S-transferase M1 gene (GSTM1) encodes a phase II enzyme responsible for detoxifying carcinogenic electrophiles. Polymorphic null forms of the gene GSTM1 lack enzyme activity and have been associated with...
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The glutathione S-transferase (GST) enzymes catalyse the conjugation of xenobiotics to glutathione. Based on reports that inherited copy number variations (CNVs) modulate some GST gene expression levels, and that the small airway epithelium (SAE) and alveolar macrophages (AMs) are involved early in the pathogenesis of smoking-induced lung disease, we asked: do germline CNVs modulate GST express...
متن کاملA soluble auxin-binding protein from Hyoscyamus muticus is a glutathione S-transferase.
We have used the photoaffinity label azido-[3H]IAA (5-N3-[7-3H]indole-3-acetic acid), a biologically active analog of indole-3-acetic acid, to identify auxin-binding proteins (ABPs) in the soluble fraction of Hyoscyamus muticus. A 25-kD polypeptide previously described (H. Macdonald, A. M. Jones, P. J. King [1991] J Biol Chem 266: 7393-7399) has now been purified to homogeneity by conventional ...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1992
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.89.1.56