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PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Open accessAbstract
Since 1922 when Wu proposed the use of the Folin phenol reagent for the measurement of proteins (l), a number of modified analytical procedures ut.ilizing this reagent have been reported for the determination of proteins in serum (2-G), in antigen-antibody precipitates (7-9), and in insulin (10).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 reagent, nevertheless, has considerable merit for certain application, but that its peculiarities and limitations need to be understood for its fullest exploitation, it has been studied with regard t.o effects of variations in pH, time of reaction, and concentration of reactants, permissible levels of reagents commonly used in handling proteins, and interfering subst.ances.Procedures are described for measuring protein in solution or after precipitation wit,h acids or other agents, and for the determination of as little as 0.2 y of protein. MethodReagents-Reagent A, 2 per cent N&OX in 0.10 N NaOH.Reagent B, 0.5 per cent CuS04.5Hz0 in 1 per cent sodium or potassium tartrabe.Reagent C, alkaline copper solution.Mix 50 ml. of Reagent A with 1 ml. of Reagent B. Discard after 1 day.Reagent D, carbonate-copper solution, is the same as Reagent C except for omission of NaOH.Reagent E, diluted Folin reagent.Titrate Folin-Ciocalteu phenol reagent ((II), Eimer and Amend, Fisher Scientific Company, New York) with NaOH t.o a phenolphthalein end-point.On the basis of this titration dilute the Folin reagent (about 2-fold) to make it 1 N in acid.Working standards may be prepared from human serum diluted IOO-to lOOO-fold (approximately 700 to 70 y per ml.).These in turn may be checked against a standard solution of crystalline bovine albumin (Armour and * Supported in part by a grant from the American Cancer Society on the recommendation of the Committee on Growth of the National Research Council.
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Metadata
- Authors
- Lowry, O., Rosebrough, N., Farr, A. L., & Randall, R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1951-11
- Volume
- 193
- Issue
- 1
- Pages
- 265-275
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1775749144
- Cited by
- 317,331
- References
- 0
- FWCI
- 30.86
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.