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: Metal donation and apo-metalloenzyme activation by stable isotopically labeled metallothionein.
    Author: Mason AZ, Perico N, Moeller R, Thrippleton K, Potter T, Lloyd D.
    Journal: Mar Environ Res; 2004; 58(2-5):371-5. PubMed ID: 15178055.
    Abstract:
    Coupled HPLC-ICP-MS has been used to quantitatively study the effects of GSSG and GSH on the ability of metallothionein (MTII) to donate essential and non-essential metals to apo-carbonic anhydrase. Stable isotopically labeled (67)Zn(3)Cd(4) MTII was used to enable Zn donated from MTII to be differentiated from extraneous sources of Zn. Transfer of both (67)Zn and Cd from MTII to apo-carbonic anhydrase was noted in the absence of either GSSG or GSH. GSSG increased the initial transfer of both Zn and Cd. Thereafter, a gradual increase in the (67)Zn content at the expense of Cd was noted over 24-h indicating continued interaction and exchange between MTII and the enzyme commensurate with the relative preferences shown by the proteins for these two metals. Although GSH also increased transfer of (67)Zn from MT it reduced the simultaneous transfer of Cd to the enzyme thereby conferring protection against Cd induced activation.
    [Abstract] [Full Text] [Related] [New Search]