Natalie Perico

California State University, Long Beach, Long Beach, California, United States

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Publications (2)5.52 Total impact

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    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 (Zn3Cd4)-Zn-67 MTII was used to enable Zn donated from MTII to be differentiated from extraneous sources of Zn. Transfer of both Zn-67 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 Zn-67 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 Zn-67 from NIT it reduced the simultaneous transfer of Cd to the enzyme thereby conferring protection against Cd induced inactivation. Fig. 1. Representative ion exchange HPLC-ICP-MS elemental profiles showing the transfer of Zn-67 and Cd-114 to apo-CA (4.09 min) from (Zn3Cd4MTII)-Zn-67 (11.05 min) in the absence (a) and presence of GSH (b) and GSSG (c). Incubations were for 1 h at 25 degrees C. The mixtures applied to the column contained a total of 25 pmol of (Zn3Cd4MTII)-Zn-67, 175 pmol of apo-CA in the presence or absence of 25 nmol of GSH or GSSG in a total volume of 50 mu l. The peak at 2.6 min eluted with the void and was tentatively identified as an oxidation product of MTII since the addition of GSSG increased (b), while GSH abolished (c), this peak.
    Full-text · Article · Jul 2005 · Marine Environmental Research
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    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.
    No preview · Article · Aug 2004 · Marine Environmental Research

Publication Stats

20 Citations
5.52 Total Impact Points

Institutions

  • 2004-2005
    • California State University, Long Beach
      • Department of Biological Sciences
      Long Beach, California, United States