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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: Protein assay in natural rubber latex was developed by using Lowry and Biuret methods for color developing followed by analysis with a laboratory designed and fabricated spectropantonometer and found that the developed method could directly be used to quantify colloidal protein in latex without precipitation and preconcentration.
Abstract: In this research, protein assay in natural rubber latex (NRL) was developed by using Lowry and Biuret methods for color developing followed by analysis with a laboratory designed and fabricated spectropantonometer. It was found that the developed method could directly be used to quantify colloidal protein in latex without precipitation and preconcentration. Therefore, this protein assay could directly be used to detect the intensity of the color developed proportional to the concentrations of protein in natural rubber latex. From the experiment, the proteins found in natural rubber are 0.037 and 0.044 %w/v by Lowry and Biuret methods, respectively. The results obtained from both color developing methods are not significantly different at 95 % confidence limit. Keywords: natural rubber latex, protein, Lowry method, Biuret method
28 Oct 2014
TL;DR: In this article, the Bradford method was used for the determination of total proteins in bovine milk dilution 1:25 to values closer to those obtained by the Kjeldahl method.
Abstract: Reliable methods for determination and quantification of total protein in food are essential information to ensure quality and safety of food trade. The objective of this study was to evaluate the linearity of calibration curves obtained from different proteins (blood serum albumin-BSA, α-LA, β-LG, αs, β and κ-CAS) with the reagent of Bradford. Comercial UHT skimmed bovine milk was analyzed for the determination of total protein using the Bradford method by reading at 595 nm. The determination of the concentrations of total milk protein was achieved by linear regression. The Bradford method showed a high sensitivity for the determination of total proteins in bovine milk dilution 1:25 to values closer to those obtained by the Kjeldahl method. The results showed that the calibration curve of standard proteins β-CN and BSA obtained better linearity with less variation in the absorbance measurements for the determination of total protein of milk.
TL;DR: In this paper, the authors compared the Biuret, Lowry, Bradford, and Mlikoscan methods used to determine the level of protein in goat's milk and compare them with the Kjeldahl method.
Abstract: The objective of this study was to correlate the Biuret, Lowry, Bradford, and Mlikoscan methods used to determine the level of protein in goat's milk and compare them with the Kjeldahl method. Milk samples collected from 18 goats of breeds Saanen (n=5), Anglo-Nubian (n=4), Pardo-alpina (n=5), and Creole (n=4) were analyzed. Correlation analyses between the different methods were performed using the Pearson test and the protein content between different breeds was compared using ANOVA. Total protein (TP) and casein (CN) concentrations obtained by all methods studied were positively correlated with the Kjeldahl method (p<0.01). The Bradford method presented the lowest correlation coefficient. All methods apart from Bradford showed significant differences in TP and CN between the Anglo-Nubian and Pardo-alpina breeds (p<0.05). The Bradford method showed significant differences in TP between the Saanen and Pardo-alpina breeds (p<0.05), and no differences were found between breeds reegarding CN. In conclusion, the Bradford method had the lowest correlation value (TP and CN) with the Kjeldahl, and the Bradford method did not show the same pattern of differences between breeds in TP and CN, as was evidenced in all other methods. Therefore, the use of the Bradford method is not recommended to determine proteins in goat’s milk.
TL;DR: In this article, a novel and highly sensitive protein assay based on the biuret reaction and using chromeazurol B, a metal chelate compound, is presented, which consists of two reagents and an automated analyzer.
01 Jan 2020
TL;DR: In this article, the proteins are dialyzed against weak salt solutions to remove the salts and sugars and the purity of these proteins is checked by SDS-PAGE, the peptide fractions are collected on the preparative HPLC and freeze lyophilized.
Abstract: The proteins are isolated from foods like wheat, milk, soybean, spinach, and rice. The isolated proteins are dialyzed against weak salt solutions to remove the salts and sugars. The proteins are estimated by Folin Lowry or Bradford method. The purity of these proteins is checked by SDS-PAGE. Simulated gastrointestinal digestion (SGID) of the isolated proteins is done through proteolytic enzymes at 37 °C for different incubation time. The hydrolysates are filtered through centrifugal filters with different molecular weight cut-off filters (MWCOF). The generated exorphins are analyzed through analytical HPLC (RP-HPLC) using a C18 column and correlated with chemically synthesized standard exorphins. The peptide fractions are collected on the preparative HPLC and freeze lyophilized. The lyophilized powder is reconstituted in a buffer and the opioid activity is assessed on isolated organ bath using GPI or MVD assay. The other reconstituted fraction is estimated for the presence of exorphins by ELISA and the data is validated through mass spectrometers like a tandem, quadrupole ion-trap (QIT), or time of flight (TOF) (MALDI-TOF/TOF).