A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.

@article{Bradford1976ARA,
  title={A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.},
  author={M. M. Bradford},
  journal={Analytical biochemistry},
  year={1976},
  volume={72},
  pages={
          248-54
        }
}
  • M. M. Bradford
  • Published 1976
  • Chemistry, Medicine
  • Analytical biochemistry
Abstract A protein determination method which involves the binding of Coomassie Brilliant Blue G-250 to protein is described. The binding of the dye to protein causes a shift in the absorption maximum of the dye from 465 to 595 nm, and it is the increase in absorption at 595 nm which is monitored. This assay is very reproducible and rapid with the dye binding process virtually complete in approximately 2 min with good color stability for 1 hr. There is little or no interference from cations… Expand
A method for quantitating nanogram amounts of soluble protein using the principle of silver binding.
TLDR
A highly sensitive and quantitative assay for measuring protein in solution based on the capacity of protein to bind silver is described, representing a 100-fold increase in sensitivity over the Coomassie brilliant blue dye-binding procedure. Expand
A rapid and reproducible assay for quantitative estimation of proteins using bromophenol blue.
  • R. Flores
  • Chemistry, Medicine
  • Analytical biochemistry
  • 1978
TLDR
A method for the quantitation of proteins in solution which involves the binding of bromophenol blue to proteins under acidic conditions has been developed and has very few interferences. Expand
Measurement of microgram quantities of protein by a generally applicable turbidimetric procedure.
  • J. Vera
  • Chemistry, Medicine
  • Analytical biochemistry
  • 1988
TLDR
A modified turbidimetric method for protein determination which involves the use of trichloroacetic acid as the precipitating agent is described and compared favorably with the most widely used protein quantitation methods in simplicity, sensitivity, and specificity. Expand
Dye-binding protein assay using a long-wave-absorbing cyanine probe.
TLDR
A simple and fast protein assay that involves the binding of water-soluble sulfonate heptamethylene cyanine to protein is described, which is very reproducible, of good color stability for at least 80 min, and sensitive at the 100 ng/mL level of human serum albumin (HSA) when a spectrophotometer with near-infrared wavelength is used to measure absorbance. Expand
A solid-phase method for the quantitation of protein in the presence of sodium dodecyl sulfate and other interfering substances.
TLDR
A simple assay for small amounts of protein that is insensitive to sodium dodecyl sulfate (SDS) or many common interfering substances including Tris and reducing sugars, which is particularly useful in the analysis of protein content of samples prior to SDS electrophoresis. Expand
Quantitation of proteins using a dye-metal-based colorimetric protein assay.
TLDR
The new Pierce 660 nm Protein Assay is very reproducible, rapid, and more linear compared with the Coomassie dye-based Bradford assay, which has a moderate protein-to-protein variation and is compatible with most detergents, reducing agents, and other commonly used reagents. Expand
A filter paper dye-binding assay for quantitative determination of protein without interference from reducing agents or detergents.
TLDR
This filter paper assay is useful for determining 100 ng to 20 micrograms of protein in the presence of ammonium sulfate, urea, thiol-reducing agents, amino acids, DNA, ionic and nonionic detergents, and acid or base. Expand
A silver-binding assay for measuring nanogram amounts of protein in solution.
  • G. Krystal
  • Chemistry, Medicine
  • Analytical biochemistry
  • 1987
TLDR
This highly sensitive assay for measuring protein in solution based on the capacity of glutaraldehyde-treated protein to bind silver has been made more sensitive, with a lower limit of detection of 5 ng, and more reproducible by supplementing protein samples with sodium dodecyl sulfate to reduce protein loss to glassware. Expand
Refinement of the Coomassie blue method of protein quantitation: A simple and linear spectrophotometric assay for ≤0.5 to 50 μg of protein
The Coomassie brilliant blue G assay for proteins described by Bradford (1976) (Anal. Biochem.72, 248) was reexamined. It was found that the extinction coefficient of the dye-protein complex solutionExpand
Methods for Measuring the Concentrations of Proteins.
Determining the concentration of protein samples generally is accomplished either by measuring the UV absorbance at 280 nm or by reacting the protein quantitatively with dyes and/or metal ionsExpand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 43 REFERENCES
A rapid, sensitive, and specific method for the determination of protein in dilute solution.
TLDR
This protein assay is described in which the sample is precipitated with trichloroacetic acid in the presence of sodium dodecylsulfate, filtered off on a Millipore membrane and stained with Amidoschwarz 10B, and its absorbance determined at 630 nm. Expand
Simple Microassay of Protein with Membrane Filter
TLDR
Protein determination by ultra-violet absorbancy may also suffer from severe interference by other chemicals and the results must be corrected for them2. Expand
Membrane Filtration for determining Protein in the Presence of Interfering Substances
TLDR
This method involves the analysis of protein precipitated by TCA and then separated from interfering substances by membrane filtration on ‘Millipore’ filters. Expand
Protein measurement with the Folin phenol reagent.
TLDR
Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein. Expand
Photometric analysis of proteins and peptides at 191-194 millimicrons.
TLDR
The light absorption band of the peptide bond at 191–194 mμ has been used for quantitative measurement of purified peptides and proteins with the Beckman DBG spectrophotometer, and in cases in which proteins cannot be analyzed in terms of nitrogen or protein weight, analysis by photometry is subject to less uncertainty than that at 280 mμ. Expand
Proteins in meat and egg products determined by dye binding.
SUMMARY— Under optimum conditions Acid Orange–12 will bind to the proteins of meat and eggs. The dye-binding capacity is somewhat greater for these products than the previously reported values forExpand
Determination of serum proteins by means of the biuret reaction.
TLDR
An investigation of the biochemical changes following experimental liver injury felt the need of a simple, rapid, and accurate method for determining the protein fractions in small amounts of serum and began with Kingsley’s biuret procedure. Expand
Interferences by sulfhydryl, disulfide reagents and potassium ions on protein determination by Lowry's method.
TLDR
The concentrations ofulfhydryl, disulfide reagents, and also potassium ions interfere with the protein determination by Lowry's method, but at moderate concentrations this interference can be overcome by running appropriate blanks. Expand
The use of Coomassie Brilliant Blue G250 perchloric acid solution for staining in electrophoresis and isoelectric focusing on polyacrylamide gels.
TLDR
A method has been developed to stain rapidly protein zones not only in standard but also in isoelectric focusing polyacrylamide gels that selectively visualizes the arginine- rich histones because of the solubility of the lysine-rich histones in PCA. Expand
Orange G dye binding for determination of protein of sow's milk.
TLDR
Equations for protein in sow's milk by Orange G dye binding procedures were: per cent protein=9.184-4.526 (absorbance) at Sensitivity 1 for samples above 6.5% protein, and per centprotein=7.317-6.061 at Sensitive 2 for samples containing 3.0 to 6.0% protein. Expand
...
1
2
3
4
5
...