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What are the advantages and disadvantages of Bradford protein assay?
Wiki User
∙ 14y ago
Advantages:
Compatible with most buffers, reagents and preparations. One step procedure that is sensitive and accurate.
Disadvantages:
Non linear correlation over large range of protein concentrations. The dye binds to surface of cuvettes so calibration curves need to be made every time. Also the dye binds to test tubes so washing after use immediate use is a must. High concentration detergents can interfere with assay.
Wiki User
∙ 14y ago
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Is the Bradford dye method of protein assay considered destructive or non destructive?
non-destructive
Advantages and disadvantages of folin-lowry assay?
advantages: although it requires no digestion, it is very sensitive. it is 10 to 20 times more sensitive than ultraviolet absorption at 289nm and it is simple Disadvantages: the amount of colour varies with different proteins, the colour is not strictly proportional to the concentration
What is protein assay?
Protein assay is the determination of concentration or total level of protein in a solution.There are various protein assays employed like bradford assay and lowry assay
Merits and demerits of Bradford assay?
Bradford protein assay is a very quick way of testing for proteins in solutions. However, presence of detergents in the solution being investigated renders this test inapplicable.
Is the Bradford dye method of protein assay considered destructive or non destructive?
non-destructive
What are the disadvantages of BCA assay?
What is better for the new students whom want to take computer course cse{computer science Engineering } OR BCA { Bachelor of Computer Applications}????? Give us Your opinion with the advantages and disadvantages !!!!
Advantages and disadvantages of folin-lowry assay?
advantages: although it requires no digestion, it is very sensitive. it is 10 to 20 times more sensitive than ultraviolet absorption at 289nm and it is simple Disadvantages: the amount of colour varies with different proteins, the colour is not strictly proportional to the concentration
To test wether a sample contains proteins what reagent should be used?
The Bradford reagent (Coomassie) is commonly used to detect if a sample contains protein. Coomassie will react with aromatic amino acids (phenylalanine, tyrosine and tryptophan) to turn from a dull red color to a bright blue color. This assay is dependant on the amount of aromatic amino acids present, but works well as a "quick and dirty" indicator of the presence of a protein. The bicinchonic acid assay (BCA assay), while more expensive than the Bradford assay, more accurately detects the presence of the peptide bond present in proteins, so it can be used to not only detect proteins which lack aromatic amino acid residues, but also can be used to more accurately determine the concentration of protein in a sample as not all proteins have the same amount of aromatic amino acids.
What is a bandshift assay?
A bandshift assay is a type of assay using gel electrophoresis, in which the mobility of a DNA or RNA probe alone is compared to its mobility in combination with a particular protein.
How the protein sample without aromatic ring containing aminoacids can be observed under spectrophotometer and at what wave length?
A general protein assay for determining protein concentrations (of proteins with no aromatic amino acids) would be using the Bradford Method. The binding of this Coomassie Brilliant Blue G-250 dye to proteins will cause a shift in the dye's maximum absorbance wavelength. The free dye is red and absorbs at 465nm, but the blue protein-bound dye can be visualized at 595nm. You will need to construct a standard curve of BSA, for example. Then use the trend line from that curve to determine your protein concentration. Reference: Bradford, M. 1976, Analytical Biochemistry, vol. 72, p. 248.
Why their is decrease in OD of Bradford protein assay method when taken OD second time?
That depends on the length of time you wait between the first and second readings. If you take them within a few minutes, the OD reading should be similar. After a while, the color fades because of the instability of the product formed in the reaction.
What is the advantages of using biuret reaction in place of measuring the absorption of the protein solution at 280 nm?
The absorption of proteins at 280nm is according to electrons from the rings on the amino acid such as His, Trp, etc. And if there is no such kind of amino acids in the protein, we might not be able to get what the amount of the protein really is. At the other hand, what makes biuret reaction work is by the copper ion reacting with the dipeptide bonds, since every amino acid has the peptide bond, it's more accurate and reasonable to use biuret reactions to determine what the amount of the protein is.
What is azocasein?
Azocasein is a chemically modified protein that was designed as a substrate for quantative assay of proteolytic enzyme activity. Hope that helped!!
What is a marker protien?
A protein marker is just that - a marker for specific proteins. This usually deals with running an experiment (assay) to determine the presence, absence, and with some markers, abundance of a specific protein
