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- W2016203973 abstract "A semi-quantitative protein assay, taking advantage of the adsorption of proteins to hydrophobic surfaces, has been developed. The test solution was serially diluted in buffer drops which had been applied to a flat polystyrene surface. After 2 min incubation the surface was tilted to a vertical position. The number of drops remaining on the surface was related to the protein concentration in the undiluted test solution. Drops containing an insufficient amount of protein ran along the surface. Of most model-proteins tested 3 μg ml−1 was reproducibly recordable. The principle of the assay was explored by determination of advancing and receding contact angles at water/air/solid interfaces. The large difference demonstrated in the advancing and receding contact angle on protein-coated polystyrene surfaces, hysteresis effect, is a hydrodynamic explanation of the phenomenon that drops containing protein hang onto the polystyrene surface when tilted. The assay was compared with the Biuret assay. A good correlation (r = 0.90) was found between the methods when the protein concentration in urine samples was determined, indicating that the assay developed in this study has a selectivity for proteins in complex solutions. However, other experiments showed interference with substances like polyethylene glycol and detergents." @default.
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- W2016203973 title "A solid-phase method for protein determination" @default.
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- W2016203973 doi "https://doi.org/10.1016/0166-6622(89)80259-8" @default.
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