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Related Concept Videos

Extraction: Advanced Methods00:56

Extraction: Advanced Methods

Metal ions can be separated from one another by complexation with organic ligands–the chelating agent– to form uncharged chelates. Here, the chelating agent must contain hydrophobic groups and behave as a weak acid, losing a proton to bind with the metal. Since most organic ligands used in this process are insoluble or undergo oxidation in the aqueous phase, the chelating agent is initially added to the organic phase and extracted into the aqueous phase. The metal-ligand complex is formed in...

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Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis
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Partial Purification and Characterization of Copper-binding Protein from Roots of Agrostis gigantea Roth.

W E Rauser1

  • 1Department of Botany and Genetics, University of Guelph, Guelph, Ontario, N1G 2W1 Canada.

Journal of Plant Physiology
|December 1, 2012
PubMed
Summary

Researchers isolated a copper-binding protein from Agrostis gigantea roots. This protein, distinct from metallothioneins, has a unique copper-cysteine ratio and composition.

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Identification of Post-translational Modifications of Plant Protein Complexes
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Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

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Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis
07:54

Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis

Published on: August 22, 2018

Identification of Post-translational Modifications of Plant Protein Complexes
10:07

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

Area of Science:

  • Biochemistry
  • Plant Physiology
  • Metalloprotein Research

Background:

  • Copper is an essential micronutrient for plants, playing vital roles in various enzymatic processes.
  • Understanding copper-binding proteins is crucial for elucidating plant responses to metal stress and nutrient uptake.
  • Agrostis gigantea, a grass species, is known for its tolerance to heavy metals, suggesting unique metal-binding mechanisms.

Purpose of the Study:

  • To isolate and characterize a novel copper-binding protein from the roots of Agrostis gigantea.
  • To determine the physicochemical properties and copper-binding characteristics of the isolated protein.
  • To investigate whether the protein exhibits characteristics similar to known copper-thioneins.

Main Methods:

  • Isolation of heat-stable proteins from Agrostis gigantea roots.
  • Chromatography using QAE-Sephadex A-25 anion exchanger for initial purification.
  • Gel filtration chromatography on Bio-Gel P-6 with high salt concentration (1 kmol m(-1) KCl) for further purification.
  • Analysis of protein composition, molecular weight, and copper content.

Main Results:

  • A heat-stable, copper-binding protein was successfully isolated from Agrostis gigantea roots.
  • The purified protein appeared as a light blue powder with an apparent molecular weight of 1700 Da.
  • The protein contained significant amounts of cysteine (11%), aspartic acid (14%), and glutamic acid (27%), with a copper content of 0.25 g atoms per mole and a Cu:cysteine ratio of 1:6.
  • Crucially, no Cu(I) indicative of Cu(I)-thiolate bonds, characteristic of Cu-thioneins, was detected, even with precautions against oxidation.

Conclusions:

  • A novel copper-binding protein, distinct from typical Cu-thioneins, has been identified in Agrostis gigantea.
  • The protein's unique composition and lack of Cu(I) suggest a different mechanism for copper binding and potential roles in copper homeostasis or detoxification in this grass species.
  • Further research is warranted to elucidate the precise structure, function, and biological significance of this metalloprotein.