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Bradford protein assay
About: Bradford protein assay is a research topic. Over the lifetime, 635 publications have been published within this topic receiving 239107 citations.
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TL;DR: This study conclusively shows a strong response of CBB to CTAB that causes a time-dependent and nearly additive interference with the Bradford assay, suggesting that both electrostatic and hydrophobic interactions are involved in the interaction of C TAB and CBB.
32 citations
TL;DR: In this paper, a modified Coomassie brilliant blue (CBB) protein assay (or Bradford method) was used to detect the amount of proteins adsorbed on the material surfaces after the pilot research for the optimal ratio of protein-to CBB-solution had been performed.
Abstract: The aim of this study is to investigate the adsorptive property of proteins on surfaces of three kinds of carbon films (DLC, CN 0.088 , and CN 0.15 ) and the medical origin of PMMA. The carbon films were first synthesized by magnetron sputtering with different deposition parameters. The surface characteristics of both the carbon films and the original samples were then measured using a contact-angle meter. A modified Coomassie brilliant blue (CBB) protein assay (or Bradford method) was used to detect the amount of proteins adsorbed on the material surfaces after the pilot research for the optimal ratio of protein- to CBB-solution had been performed. The results of the pilot research show that the optimal ratio of protein- to CBB-solution is 1:3, and the protein adsorption results show that the sequence amounts of proteins adsorbed on four kinds of surfaces are DLC > CN 0.088 > PMMA > CN 0.15 . This was the same as the hydrophobicity sequence of four kinds of surfaces obtained from the contact-angle test. However, the ratio of albumin to IgG ( R A/I ) adsorbed on the four surfaces has an order of PMMA > CN 0.15 > DLC > CN 0.088 , which indicates the anti-thrombogenicity property of the four kinds of surfaces.
31 citations
TL;DR: The results have suggested this TCA/SDS precipitation method to be useful for quantitating dilute protein samples containing high concentrations of detergents and other reagents commonly employed in studying membrane proteins.
31 citations
TL;DR: It is demonstrated that the dimethylation of lysyl ε-amines does not affect the proteins' molar extinction coefficients at 280 nm, and the implications for the analysis of biologically methylated samples are discussed.
31 citations
TL;DR: The developed method using Coomassie blue binding can be used for the quantification of cationic groups in a macromolecule grafted onto a solid surface and it is demonstrated that one Coomassi blue molecule interacts with only one single protonated group.
Abstract: BACKGROUND: The aim of the work reported was to develop a procedure using 96-well microtiter plates for the easy determination of protonated groups of compounds including linear poly(amino acid)s and dendritic polymers divided into dendrigraft and dendrimeric structures. This study is a prerequisite step for the quantification of protonated groups in a macromolecule grafted onto a solid surface. RESULTS: The procedure was developed from the modified Bradford protein assay and incorporates several modifications that enable one to determine available amino groups (or even other cationic groups) present on the polyresidues backbone, all withinfiveminutes.BasedontheAthertonmathematicalmodel,weevaluatedthemaximalnumberofCoomassiebluebinding sites on linear, dendrigraft or even dendrimeric structures. CONCLUSION: The mean calculated percentage of occupied sites on a given macromolecule led us to demonstrate that one Coomassie blue molecule interacts with only one single protonated group. Consequently, the developed method using Coomassie blue binding can be used for the quantification of cationic groups in a macromolecule grafted onto a solid surface. c � 2009 Society of Chemical Industry
31 citations