BAL = British Anti Lewisite. You may know it as dimercaprol. Just another chelator, mostly used for arsenic, lead, gold and inorganic mercury poisoning, but can be used for other metals.
Danielle
Danielle
21 - 40 of 41 Posts
I'd hammer out justice, I'd hammer out freedom 
Complexation and flocculation of metals occurs with organic material. For instance, EDTA is often used in chemical procedures to bond metals. Metals bound in such a manner can either be settled to the floor of the ponds and recycled as the organic matter is decomposed, or taken directly into the food chain. The metals can be made relatively inert as long as the organic material is stable. However, metals are particularly rapidly assimilated into the food chain when bound to organic material. In decreasing order of strength Pb, Cu, Ni, Co, Zn, Cd, Fe, Mn, Mg form associations with humic material.
http://www.deltaenvironmental.com.au/archives/saltwetland/saltwetl.htm
BTW it's bacterial driven.
"MetalsRUs"
Complexation and flocculation of metals occurs with organic material. For instance, EDTA is often used in chemical procedures to bond metals. Metals bound in such a manner can either be settled to the floor of the ponds and recycled as the organic matter is decomposed, or taken directly into the food chain. The metals can be made relatively inert as long as the organic material is stable. However, metals are particularly rapidly assimilated into the food chain when bound to organic material. In decreasing order of strength Pb, Cu, Ni, Co, Zn, Cd, Fe, Mn, Mg form associations with humic material.
http://www.deltaenvironmental.com.au/archives/saltwetland/saltwetl.htm
BTW it's bacterial driven.
"MetalsRUs"
"If I had a hammer....there'd be no more folk singers."
Billy Connelly~comedian
Back to what I was saying.... In what state does the copper exist within the environment?
If we define the state of coppers existance within the inorganic material environment, we can establish some criteria in which to determine the propper approach for it's removal....
By telling me that since I ate a penny and pissed in the lake that when the fish dies that swam though my pee, his decomposed body is going to leave behind the minute remnats of the penny and therefore inflict more harm upon the next inhabitants is moot.... We're talking about inorganics here...
If we define the state of coppers existance within the inorganic material environment, we can establish some criteria in which to determine the propper approach for it's removal....
By telling me that since I ate a penny and pissed in the lake that when the fish dies that swam though my pee, his decomposed body is going to leave behind the minute remnats of the penny and therefore inflict more harm upon the next inhabitants is moot.... We're talking about inorganics here...
The problem is that the copper does not leach out of the glass quickly or easily. If it did, then a few days of water changes would be enough to solve the problem.Newfiemom said:It does only bind in solution. My thought was that the EDTA would complex any free copper, and then the bound copper (in the glass, etc) would leach out into solution to reestablish the "equilibrium", and get complexed, causing more copper to leach out...etc. I can write out some chemical equations for this, but I don't want to be responsible for any seizures that could occur among unsuspecting readers.
Which acid have you heard of using? Nitric would do it, but would probably cloud the glass in the process if you weren't careful.
Hydrochloric acid for acid washing the tank.
Hmmmmmm.... This is interesting...
Blue or 'type-1' copper proteins are small proteins which bind a single copper atom and which are characterized by an intense electronic absorption band near 600 nm [MEDLINE:84135769], [MEDLINE:93164266]. The most well known members of this class of proteins are the plant chloroplastic plastocyanins, which exchange electrons with cytochrome c6, and the distantly related bacterial azurins, which exchange electrons with cytochrome c551. This family of proteins also includes amicyanin from bacteria such as Methylobacterium extorquens or Thiobacillus versutus that can grow on methylamine; auracyanins A and B from Chloroflexus aurantiacus [MEDLINE:92202194]; blue copper protein from Alcaligenes faecalis; cupredoxin (CPC) from cucumber peelings [MEDLINE:93106154]; cusacyanin (basic blue protein; plantacyanin, CBP) from cucumber; halocyanin from Natrobacterium pharaonis [MEDLINE:94253046], a membrane associated copper-binding protein; pseudoazurin from Pseudomonas; rusticyanin from Thiobacillus ferrooxidans [MEDLINE:91348256]; stellacyanin from the Japanese lacquer tree; umecyanin from horseradish roots; and allergen Ra3 from ragweed. This pollen protein is evolutionary related to the above proteins, but seems to have lost the ability to bind copper. Although there is an appreciable amount of divergence in the sequences of all these proteins, the copper ligand sites are conserved.
Blue or 'type-1' copper proteins are small proteins which bind a single copper atom and which are characterized by an intense electronic absorption band near 600 nm [MEDLINE:84135769], [MEDLINE:93164266]. The most well known members of this class of proteins are the plant chloroplastic plastocyanins, which exchange electrons with cytochrome c6, and the distantly related bacterial azurins, which exchange electrons with cytochrome c551. This family of proteins also includes amicyanin from bacteria such as Methylobacterium extorquens or Thiobacillus versutus that can grow on methylamine; auracyanins A and B from Chloroflexus aurantiacus [MEDLINE:92202194]; blue copper protein from Alcaligenes faecalis; cupredoxin (CPC) from cucumber peelings [MEDLINE:93106154]; cusacyanin (basic blue protein; plantacyanin, CBP) from cucumber; halocyanin from Natrobacterium pharaonis [MEDLINE:94253046], a membrane associated copper-binding protein; pseudoazurin from Pseudomonas; rusticyanin from Thiobacillus ferrooxidans [MEDLINE:91348256]; stellacyanin from the Japanese lacquer tree; umecyanin from horseradish roots; and allergen Ra3 from ragweed. This pollen protein is evolutionary related to the above proteins, but seems to have lost the ability to bind copper. Although there is an appreciable amount of divergence in the sequences of all these proteins, the copper ligand sites are conserved.
I vote for Jay to try it.... cause I ain't gonna dose a tank with copper to try it out...
Or you can try cucumber rinds...
Read the info I posted...
but in a nutshell.....
Blue or 'type-1' copper proteins are small proteins which bind a single copper atom and which are characterized by an intense electronic absorption band near 600 nm. This family of proteins also includes cupredoxin (CPC) from cucumber peelings; cusacyanin (basic blue protein; plantacyanin, CBP) from cucumber;
It'd be worth chopping up a bunch of cucumber, putting it in a filter bag and soaking it with something......
Read the info I posted...
but in a nutshell.....
Blue or 'type-1' copper proteins are small proteins which bind a single copper atom and which are characterized by an intense electronic absorption band near 600 nm. This family of proteins also includes cupredoxin (CPC) from cucumber peelings; cusacyanin (basic blue protein; plantacyanin, CBP) from cucumber;
It'd be worth chopping up a bunch of cucumber, putting it in a filter bag and soaking it with something......
That would actually be a pretty neat solution. It is possible that the proteins have to be extracted before they can strongly bind the Copper in solution, but it is also possible that they don't. Did any of the papers say if the copper-binding property was utilized biologically? If so, the binding site might already be occupied, and it wouldn't be so simple. But definitely worth a try.Buzz_Hog said:Or you can try cucumber rinds...
I am really curious to know what is in the commercial product...there are lots of ligands that could form really strong bonds with a metal.
21 - 40 of 41 Posts
