These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: [Cloning and characterization of a novel glutathione transferase gene from Penicillium chrysogenum].
    Author: Zhang Y, Wang FQ, Zheng GZ, Dai M, Liu J, Zhao Y, Ren ZH, Zhao BH, Jia Q.
    Journal: Sheng Wu Gong Cheng Xue Bao; 2007 Jul; 23(4):618-22. PubMed ID: 17822032.
    Abstract:
    Glutathione transferases (GSTs) are a family of multifunctional proteins that mainly catalyze the conjugation of intracellular glutathione (GSH) to a wide variety of endogenous and exogenous electrophilic compounds. GSTs play important roles in stress tolerance and in the detoxification metabolism in organisms. A novel GST gene, Pc gstB, was cloned from penicillin producing fungus Penicillium chrysogenum using RT-PCR. The open reading frame (ORF) of Pc gstB was 651 bp and encoded a peptide of 216 residues. The deduced amino acids sequence had conserved GST domain and showed 65% identity to the characterized Aspergillus fumigutus gstB. The entire ORF of Pc gstB was inserted into vector pTrc99A and transformed into Escherichia coli DH5alpha. Recombinant PcGstB was overexpressed and its GST activity toward substrate 1-chloro-2,4-dinitrobenzene (CDNB) was validated.
    [Abstract] [Full Text] [Related] [New Search]