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: Thioltransferase can utilize cysteamine as same as glutathione as a reductant during the restoration of cystamine-treated glucose 6-phosphate dehydrogenase activity.
    Author: Terada T.
    Journal: Biochem Mol Biol Int; 1994 Oct; 34(4):723-7. PubMed ID: 7866298.
    Abstract:
    Glucose 6-phosphate dehydrogenase (G6PD) [EC 1.1.1.49] is inactivated by the incubation with cystamine very efficiently, but not by oxidized glutathione. This inactivation advanced following the incubation-time and concentration of cystamine. The inactivated-G6PD is restored its activity by the treatment of thioltransferase with 1 mM cysteamine or reduced glutathione (GSH) much more effectively than only by thiols. For the first time, we suggested thioltransferase can utilize cysteamine in stead of GSH during its thiol/disulfide exchange reaction activity.
    [Abstract] [Full Text] [Related] [New Search]