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.read more
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Journal ArticleDOI
Increasing the amount of phosphoric acid enhances the suitability of Bradford assay for proteomic research
TL;DR: Results show that lysis buffer not only causes background interference but also affects the protein–dye chromogenic process and the sensitivity of the Bradford assay to proteins in lysis buffers was increased, and the interference delivered by lysisbuffer was considerably reduced.
Journal ArticleDOI
Cloning and functional expression of Citrobacter amalonaticus Y19 carbon monoxide dehydrogenase in Escherichia coli
Balaji Sundara Sekar,Subramanian Mohan Raj,Eunhee Seol,Satish Kumar Ainala,Jung-Eun Lee,Sunghoon Park +5 more
TL;DR: CODH and the required maturation proteins from the novel facultative anaerobic bacterium Citrobacter amalonaticus Y19 were cloned and heterologously expressed in Escherichia coli, suggesting that the native hydrogenases present in E. coli could not substitute the Y19 CO–H 2 ase for CO-dependent H 2 production.
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The effects of short- and long-term diet supplementation with Iranian propolis on the growth and immunity in rainbow trout (Oncorhynchus mykiss)
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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.
S.M. Read,D. H. Northcote +1 more
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.