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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: A new and simple one-reagent method for general protein assay that makes use of one of two new reactive labeling reagents presented here, referred to as pyrylium [Py] labels, which can be applied for both photometric and fluorometric protein assays at near neutral pHs at room temperature.
56 citations
TL;DR: This study compared and normalized quantitative values from two models for protein quantitation, where the residues in the protein that bind to anionic Coomassie Brilliant Blue G-250 comprise either Arg and Lys (Method 1, M1) or Arg, Lys, and His (Method 2, M2).
55 citations
TL;DR: The new Pierce 660 nm Protein Assay is very reproducible, rapid, and more linear compared with the Coomassie dye-based Bradford assay, which has a moderate protein-to-protein variation and is compatible with most detergents, reducing agents, and other commonly used reagents.
55 citations
TL;DR: The addition of protein to a sub-threshold amount of SDS results in the formation of a green color measurable as an increase in absorbance at 700 nm, in contrast to the blue color measured at 595 nm in the standard assay.
54 citations
TL;DR: The use of Nano Orange, a fluorometric assay, is described to quantitatively assess the adsorption of bovine fibrinogen and albumin onto model hydrophilic and hydrophobic surfaces and the calibration of previously unquantifiable data obtained on the same surfaces is demonstrated.
Abstract: Protein adsorption is of major and widespread interest, being useful in the fundamental understanding of biological processes at interfaces through to the development of new materials. A number of techniques are commonly used to study protein adhesion, but few are directly quantitative. Here we describe the use of Nano Orange, a fluorometric assay, to quantitatively assess the adsorption of bovine fibrinogen and albumin onto model hydrophilic (OH terminated) and hydrophobic (CH3 terminated) surfaces. Results obtained using this method allowed the calibration of previously unquantifiable data obtained on the same surfaces using quartz crystal microbalance measurements and an amido black protein assay. Both proteins were found to adsorb with higher affinity but with lower saturation levels onto hydrophobic surfaces. All three analytical techniques showed similar trends in binding strength and relative amounts adsorbed over a range of protein concentrations, although the fluorometric analysis was the only me...
54 citations