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Book ChapterDOI

The Bradford Method for Protein Quantitation

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TLDR
A rapid and accurate method for the estimation of protein concentration is essential in many fields of protein study, but is susceptible to interference from a wide range of compounds commonly present in biological extracts.
Abstract
A rapid and accurate method for the estimation of protein concentration is essential in many fields of protein study. The Lowry method ( Chapter 1 in vol. 1 of this series) has been widely used, but is susceptible to interference from a wide range of compounds commonly present in biological extracts. Although interference can be avoided by trichloracetic acid precipitation of the protein prior to assay, this lengthens the procedure.

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Mass spectrometry quantification of beef and pork meat in highly processed food: Application on Bolognese sauce

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Paracoccidioides brasiliensis 87-Kilodalton Antigen, a Heat Shock Protein Useful in Diagnosis: Characterization, Purification, and Detection in Biopsy Material via Immunohistochemistry

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Co-production of hydrogen and ethanol from glucose in Escherichia coli by activation of pentose-phosphate pathway through deletion of phosphoglucose isomerase ( pgi ) and overexpression of glucose-6-phosphate dehydrogenase ( zwf ) and 6-phosphogluconate dehydrogenase ( gnd )

TL;DR: Two important biofuels, ethanol and H2, could be successfully co-produced at high yields close to their theoretical maximums and the attempt to delete the ED pathway in the Δpgi mutant to operate the PP pathway as the sole glycolytic route was unsuccessful.
References
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Journal ArticleDOI

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

TL;DR: 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 with little or no interference from cations such as sodium or potassium nor from carbohydrates such as sucrose.
PatentDOI

Measurement of protein using bicinchoninic acid

TL;DR: This new method maintains the high sensitivity and low protein-to-protein variation associated with the Lowry technique and demonstrates a greater tolerance of the bicinchoninate reagent toward such commonly encountered interferences as nonionic detergents and simple buffer salts.
Journal ArticleDOI

A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250

TL;DR: An assay for proteins in solution that depends on the conversion of Coomassie brilliant blue G250 in dilute acid from a brownish-orange to an intense blue color has high reproducibility and can detect less than 1.0 μg of albumin.
Journal ArticleDOI

Refinement of the coomassie blue method of protein quantitation. A simple and linear spectrophotometric assay for less than or equal to 0.5 to 50 microgram of protein.

TL;DR: The Coomassie brilliant blue G assay for proteins described by Bradford (1976) (Anal Biochem72, 248) was reexamined and it was found that the extinction coefficient of the dye-protein complex solution remained constant over the protein concentration range of 08 to 10 μg/ml of solution.
Journal ArticleDOI

Minimization of variation in the response to different proteins of the Coomassie blue G dye-binding assay for protein.

TL;DR: Modifications to the Coomassie blue G dye-binding assay for protein are described which remove much of the variation previously observed in the response of this assay to different proteins.
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