Talk:Lowry protein assay

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Latest comment: 12 years ago3 comments3 people in discussion

The method combines the reactions of cupric ions with the peptide bonds under alkaline conditions (the Biuret method) with the oxidative of aromatic protein residues. The Lowry method is sensitive to protein concentrations as low as 20 ug/mL. The disadvantage of this method is the long incubation time and there are often interferences with commonly used buffers. This method is also subject to protein-to-protein variation due to the correlation of colour intensity dependent on the content of tyrosine and tryptophan in the protein.

Bad redir. Right now "Folin's reagent" sends to "Folin's reagent" - This should not be confused with Folin-Ciocalteu reagent, which is a mixture of sodium tungstate and sodium molybdate that is used to detect phenolic compounds. It should sends to "Folin-Ciocalteu reagent". Maybe I'll fix it later. I don't have much time right now. Anhelli. —Preceding unsigned comment added by 77.254.198.184 (talk) 23:52, 8 February 2009 (UTC)Reply

Fixed it. Not sure I did it right, though. Philmaster (talk) 10:53, 30 September 2009 (UTC)Reply

I'd like to suggest that the Lowry protein assay be described as a chemical assay, it is not a biochemical reaction. Acleron (talk) 12:32, 16 August 2012 (UTC)Reply

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