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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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Patent•
27 May 1987TL;DR: In this paper, a quantitative assay for an analyte which comprises contacting a sample containing a analyte with a solid phase support to immobilize said analyte, following by indirectly quantitating the presence of bound analyte by titrating the unoccupied binding sites with a titrating protein which is detectably labeled.
Abstract: The invention relates to a quantitative assay for an analyte which comprises contacting a sample containing an analyte with a solid phase support to immobilize said analyte, following by indirectly quantitating the presence of bound analyte by titrating the unoccupied binding sites with a titrating protein which is detectably labeled.
5 citations
Patent•
03 Feb 2016
TL;DR: In this paper, a method for detecting differential protein produced by action between alpinetin or cardamonin and serum is presented. But the method is not suitable for the detection of proteins produced by protein aggregation.
Abstract: The invention provides a method for detecting differential protein produced by action between alpinetin or cardamonin and serum. The method comprises the following steps: (1) shaking up serum protein and alpinetin or cardamonin with the concentration of 1.0*10 mol/L-3.0*10 mol/L and cultivating at the constant temperature; (2) removing highly-abundant proteins according to the steps of a serum albumin scavenger; (3) quantifying an obtained protein sample by use of the Bradford method; (4) performing isoelectric focusing according to the protein loading quantity of 1300 [mu]g/24 cm of a rubber strip; (5) transferring for polyacrylamide gel electrophoresis after balancing of the rubber strip; (6) after finish of electrophoresis, performing Coomassie brilliant blue staining, decolorization, storage and scanning analysis; (7) performing enzymolysis and mass spectrum identification on differential protein spots.
5 citations
TL;DR: In this article, the protein component of three different kinds of raw materials used for dry pet food production, i.e., chicken, pork, and salmon, was analyzed using the traditional Kjeldahl method and near-infrared (NIR) spectroscopy, while the qualitative analysis was performed through SDS-PAGE, followed by Coomassie Blue staining.
Abstract: The majority of dry pet food currently on the market is produced using fresh meats (FMs) and especially meat meals (MMs) as the main protein source. The transport and storage conditions of the raw materials, together with thermal and mechanical treatments in the case of MMs, may result in undesirable alterations of food products and their protein content. This study was conducted to analyze the protein component of three different kinds of raw materials used for dry pet food production, i.e., chicken, pork, and salmon. The quantitative analysis of the protein component was determined using the traditional Kjeldahl method and near-infrared (NIR) spectroscopy, and an alternative method, i.e., the Bradford assay, while the qualitative analysis was performed through SDS-PAGE, followed by Coomassie Blue staining. The amino acid (AA) profile was also evaluated by quadrupole time-of-flight liquid chromatography/mass spectrometry (Q-TOF LC/MS). In addition, the digestibility was tested through in vitro gastric and small intestine digestion simulation. Statistical analysis was performed by the Student's t-test, and data are reported as mean ± SEM, n = 10 (p < 0.05). The results showed that the MMs are lower in quality compared to FMs, both in terms of protein bioavailability and digestibility, having a lower soluble protein (SP) content (chicken MM = 8.6 g SP/100 g dry sample; pork MM = 6.2 g SP/100 g dry sample; salmon MM = 7.9 g SP/100 g dry sample) compared to FMs (chicken FM = 14.6 g SP/100 g dry sample; pork FM = 15.1 g SP/100 g dry sample; salmon FM = 13.7 g SP/100 g dry sample). FMs appear, therefore, to be higher-quality ingredients for pet food production. Moreover, the Bradford assay proved to be a quick and simple method to better estimate protein bioavailability in the raw materials used for dry pet food production, thanks to its correlation with the in vitro digestibility.
5 citations
TL;DR: Cyclic glucose oligomers known as cyclodextrins were found to interfere in the quantitation of micro amounts of protein by the Bradford method, and preliminary results showed a similar interference in the bicinchoninic acid and Lowry protein assays.
5 citations
TL;DR: In this article, a preliminary study of using maleic anhydride copolymer for protein binding has been carried out, which revealed that proteins can be successfully immobilized onto the film surface via covalent linkage.
Abstract: A preliminary study of using maleic anhydride copolymer for protein binding has been carried out. The polymeric films were prepared by compression of the purified resin and annealing the film to induce efficient back formation of the anhydride groups. The properties of the film surface were analyzed by attenuated total reflection Fourier transforms infrared spectroscopy and water contact angle measurements. The protein content was determined by Bradford assay. To obtain optimum conditions, immersion time for protein binding was examined. Results revealed that proteins can be successfully immobilized onto the film surface via covalent linkage. The efficiency of the covalent binding of the extractable protein to maleic anhydride-polyethylene film was estimated at 69.87 μg/cm2, although the film had low anhydride content (3%) on the surface.
5 citations