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Related Experiment Videos

pNiXa, a Ni(2+)-binding protein in Xenopus oocytes and embryos, shows identity to Ep45, an estrogen-regulated hepatic

B L Beck1, D C Henjum, K Antonijczuk

  • 1Department of Laboratory Medicine, University of Connecticut School of Medicine, Farmington 06030.

Research Communications in Chemical Pathology and Pharmacology
|July 11, 1992
PubMed
Summary

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A novel protein, pNiXa, found in Xenopus embryos, binds strongly to nickel (Ni2+). This protein may be a key target in nickel-induced developmental defects (teratogenesis).

Area of Science:

  • Biochemistry
  • Developmental Biology
  • Toxicology

Background:

  • A nickel-binding protein, pNiXa, was identified in Xenopus embryos.
  • pNiXa belongs to the serpin superfamily and shares similarities with Ep45, an estrogen-regulated hepatic serpin.
  • The protein contains an (HX)n-motif, a feature also found in eukaryotic transcription factors.

Purpose of the Study:

  • To characterize the biochemical properties of pNiXa.
  • To investigate the potential role of pNiXa in nickel-induced teratogenesis.

Main Methods:

  • Isolation of pNiXa from Xenopus oocytes using Ni-affinity chromatography.
  • Analysis of pNiXa's amino acid sequence and its relation to known proteins.
  • Assay of pNiXa's inhibitory activity against alpha-chymotrypsin.

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Main Results:

  • Purified, nondenatured pNiXa demonstrated inhibitory activity against bovine alpha-chymotrypsin.
  • pNiXa exhibits high avidity for Ni(2+).
  • The protein is present in Xenopus embryos during periods of nickel susceptibility.

Conclusions:

  • pNiXa is a nickel-binding protein with enzymatic inhibitory properties.
  • The presence and properties of pNiXa suggest it is a molecular target in nickel-induced teratogenesis in Xenopus embryos.