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Life is short, the art long. ~Hippocrates c.460 - 357 BC. Greek Physician and the Father of Medicine.
The Lowry protein assay method for protein concentration determination is one of the most venerable and widely-used protein assays. The Lowry method was first described in 1951 by Lowry et al. (Lowry et al., 1951).
Hydrolysis is probably the most accurate method of determining protein concentration followed by amino acid analysis. Most other methods are sensitive to the
amino acid composition of the protein, and absolute concentrations cannot be obtained. The Lowry procedure is sensitive, and is moderately constant from protein to protein. The Lowry protein estimation has been so widely used that it is a completely acceptable alternative to a rigorous absolute determination in almost all circumstances in which protein mixtures or crude extracts are involved.
The method is based on both the Biuret reaction, in which the peptide bonds of
proteins react with copper under alkaline conditions to produce Cu+, which reacts with
the Folin reagent, and the Folin–Ciocalteau reaction, which is poorly understood but in
essence phosphomolybdotungstate is reduced to heteropolymolybdenum blue by the
copper-catalyzed oxidation of aromatic amino acids. The reactions result in a strong
blue color, which depends partly on the tyrosine and tryptophan content. The method is
sensitive down to about 0.01 mg of protein/mL, and is best used on solutions with
concentrations in the range 0.01–1.0 mg/mL of protein.
The Lowry method for protein concentration determination is widely used, however can be subject to interference by many substances and chemicals.
Chemicals that are known to interefere with the Lowry Assay:
Lowry et al. J. Biol. Chem. 193: 265-275 (1951)
Lowry Method Protocol
Protein Concentration Protocol
Bradford Method
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