A study of the mechanisms of divalent copper binding to a modified cellulose adsorbent

2010 ◽  
pp. NA-NA
Author(s):  
David William O'Connell ◽  
Balazs Aszalos ◽  
Colin Birkinshaw ◽  
Thomas Francis O'Dwyer
Keyword(s):  
Copper Binding ◽  
Divalent Copper ◽  
Cellulose Adsorbent ◽  
Modified Cellulose

scholarly journals Removal of Lead(II) Ions from Aqueous Solutions Using a Modified Cellulose Adsorbent

2006 ◽  
Vol 24 (4) ◽  
pp. 337-348 ◽  
Author(s):  
David W. O'Connell ◽  
Colin Birkinshaw ◽  
Thomas F. O'Dwyer
Keyword(s):  
Aqueous Solutions ◽  
Cellulose Adsorbent ◽  
Modified Cellulose

A modified cellulose adsorbent for the removal of nickel(II) from aqueous solutions

2006 ◽  
Vol 81 (11) ◽  
pp. 1820-1828 ◽  
Author(s):  
David W O'Connell ◽  
Colin Birkinshaw ◽  
Thomas F O'Dwyer
Keyword(s):  
Aqueous Solutions ◽  
Cellulose Adsorbent ◽  
Modified Cellulose

The Research Progress of the Modified Cellulose Magnetic Microspheres Adsorption of Heavy Metal

2013 ◽  
Vol 675 ◽  
pp. 289-295 ◽  
Author(s):  
Jia Sun ◽  
Xin Zhong Liu ◽  
Lei Peng
Keyword(s):  
Heavy Metal ◽  
Magnetic Microspheres ◽  
Research Progress ◽  
Magnetic Microsphere ◽  
Adsorption Technology ◽  
Magnetic Adsorption ◽  
Cellulose Adsorbent ◽  
Modified Cellulose

The modified cellulose magnetic microsphere is magnetized on the modified cellulose. It combines the properties of the modified cellulose and the advantages of the magnetic adsorption technology together. This paper summarizes the method of preparation of modified cellulose magnetic microsphere and application of its adsorption of heavy metal. Further, this article raises the improvement methods to obtain the better performance of the finished product, thereby enhancing the cellulose adsorbent flexibility and breadth of application.

Metallic prions

2004 ◽  
Vol 71 ◽  
pp. 193-202 ◽  
Author(s):  
David R Brown
Keyword(s):  
Prion Protein ◽  
Binding Capacity ◽  
Normal Function ◽  
Transmissible Spongiform Encephalopathies ◽  
Published Data ◽  
Normal Brain ◽  
Copper Binding ◽  
Loss Of Function ◽  
Spongiform Encephalopathies ◽  
The Brain

Prion diseases, also referred to as transmissible spongiform encephalopathies, are characterized by the deposition of an abnormal isoform of the prion protein in the brain. However, this aggregated, fibrillar, amyloid protein, termed PrPSc, is an altered conformer of a normal brain glycoprotein, PrPc. Understanding the nature of the normal cellular isoform of the prion protein is considered essential to understanding the conversion process that generates PrPSc. To this end much work has focused on elucidation of the normal function and activity of PrPc. Substantial evidence supports the notion that PrPc is a copper-binding protein. In conversion to the abnormal isoform, this Cu-binding activity is lost. Instead, there are some suggestions that the protein might bind other metals such as Mn or Zn. PrPc functions currently under investigation include the possibility that the protein is involved in signal transduction, cell adhesion, Cu transport and resistance to oxidative stress. Of these possibilities, only a role in Cu transport and its action as an antioxidant take into consideration PrPc's Cu-binding capacity. There are also more published data supporting these two functions. There is strong evidence that during the course of prion disease, there is a loss of function of the prion protein. This manifests as a change in metal balance in the brain and other organs and substantial oxidative damage throughout the brain. Thus prions and metals have become tightly linked in the quest to understand the nature of transmissible spongiform encephalopathies.

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