Protein measurement with the Folin phenol reagent.

  title={Protein measurement with the Folin phenol reagent.},
  author={Oliver H. Lowry and Nira J. Rosebrough and Angie L Farr and R. J. Randall},
  journal={The Journal of biological chemistry},
  volume={193 1},
Since 1922 when Wu proposed the use of the Folin phenol reagent for the measurement of proteins, a number of modified analytical procedures utilizing this reagent have been reported for the determination of proteins in serum, in antigen-antibody precipitates, and in insulin. Although the reagent would seem to be recommended by its great sensitivity and the simplicity of procedure possible with its use, it has not found great favor for general biochemical purposes. In the belief that this… Expand
Determination of proteins and sulfobetaine with the Folin-phenol reagent.
This paper describes a method for the quantitative analysis of solutions containing a mixture of proteins and sulfobetaine, essentially following the method of O. Randall (1951), where the absorbances of the protein fraction are read while that of the detergent solution is read at 342 nm. Expand
Comparison of the phenol-reagent and bromsulfalein-binding methods for determination of protein and its measurement in mast cells.
A critical comparison of the phenol-reagent and bromsulfalein-binding methods for the determination of protein revealed no significant difference in sensitivity or reproducibility, but additional chemical differences between the normal and neoplastic mast cells were shown. Expand
A new colorimetric technique for the estimation of vitamin C using Folin phenol reagent.
A new colorimetric technique for the estimation of ascorbic acid by using Folin phenol reagent has been developed and has been found to be stable up to 18 h and almost 100% efficient. Expand
Abstract A study of the applicability of a colorimetric biuret procedure for protein determination to a variety of biological preparation has revealed that the practice of using this procedure isExpand
Review of the Folin phenol protein quantitation method of Lowry, Rosebrough, Farr and Randall.
  • G. Peterson
  • Chemistry, Medicine
  • Analytical biochemistry
  • 1979
The method of Lowry and coworkers combined the use of copper, as suggested by Herriott, with the Folin phenol method, which originated from the work of Wu, to produce a more reliable and sensitive protein analysis. Expand
Simple Microassay of Protein with Membrane Filter
Protein determination by ultra-violet absorbancy may also suffer from severe interference by other chemicals and the results must be corrected for them2. Expand
A rapid, sensitive, and specific method for the determination of protein in dilute solution.
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
Interference by carbohydrate and other substances in the estimation of protein with the Folin-Ciocalteu reagent.
The literature on this subject does not warn against the positive interference exhibited by most sugars in low concentration after exposure to hot alkali or acid despite the fact that the “molybdate blue” reaction of sugars is well known and is the basis of a clinical assay for blood glucose. Expand
Measurement and characterization of proteins by color reactions.
Two of the more sensitive methods for the determination of protein, one involving reduction of Folin's heteropolyphosphate reagent and the other, binding of a sulfonphthalein dye, have been investigated and show that different proteins cover a wide range of values in each case and that there is no uniform correlation between the two parameters measured. Expand
Optimization of Folin--Ciocalteu Reagent concentration in an automated Lowry protein assay.
The quantity of color developed in the assay was found to be strongly dependent on the concentration of the Folin-Ciocalteu phenol reagent, and color yield peaked sharply at a reagent concentration 40% lower than that used in the Lowry procedure. Expand