Showing papers on "Bradford protein assay published in 1988"
TL;DR: A technique for determining the amount of thermally denatured, insoluble protein is described, which can measure protein concentrations as small as 10 micrograms, typically with standard deviations of 3%, thus comparing favorably with the standard Bradford assay.
87 citations
TL;DR: The results indicate that it is not possible to separate patients with and without gallstones on the basis of the total protein concentration of gallbladder bile, and three protein assays were evaluated.
65 citations
TL;DR: This assay compares favorably to other assay procedures in terms of rapidity, sensitivity, expense, and lack of interference by many laboratory reagents, although like the others it suffers from the drawback of differences in response of different proteins, which is inherent in dye-binding assays.
59 citations
TL;DR: An in vitro assay based on the capacity of angiogenin to bind placental ribonuclease inhibitor (PRI) is developed, which is less tedious and more versatile than existing procedures that measure blood vessel growth or cleavage of rRNA.
50 citations
Patent•
06 Jun 1988TL;DR: In this article, a new and improved method and composition for determining the presence and concentration of low to trace amounts of proteins such as albumin, in a test sample, such as urine.
Abstract: A new and improved method and composition for determining the presence and concentration of low to trace amounts of proteins, such as albumin, in a test sample, such as urine. The method includes using a reagent composition capable of interacting with low to trace amounts of proteins to produce a visually or instrumentally detectable and/or measurable response. The method can be used in wet assays or in dry test strip assays, wherein the reagent composition is incorporating into a carrier matrix. The new and improved reagent composition, comprising a dye, such as a polyhydroxybenzenesulfonephthalein-type indicator, like pyrocatechol violet; a tungstate, such as ammonium tungstate; and, if necessary, a suitable buffer, is incorporated into the carrier matrix to provide sufficient sensitivity to low to trace protein levels and sufficient color resolution between low to trace protein levels, thereby affording an accurate and trustworthy protein assay of test samples having a low protein concentration.
20 citations
TL;DR: Underestimation of avidin and streptavidin by the Bradford method can be alleviated by carrying out the reaction at 100 degrees C for 10-15 min, and the protein values thus obtained match very well with those of biotin-binding assays.
8 citations
TL;DR: This method is effective for the determination of proteins in minute non-green and green plant tissue, and is especially designed for vegetative and floral shoot apices, and the primordia of inflorescences.
Abstract: A method is described for estimating proteins in the same plant tissue sample that is solubilized for separation by two-dimensional polyacrylamide gel electrophoresis. The method uses a modified bicinchoninic acid (BCA) protein assay procedure and a modified standard urea solubilization buffer to estimate microgram values of unknown protein concentration, in the presence of 9 M urea and 4% Nonidet P-40, from a linear standard curve. A method for a quantitative determination of protein concentration by BCA in a sample containing 9 M urea and 4% Nonidet P-40 is also described. This method is effective for the determination of proteins in minute non-green and green plant tissue, and is especially designed for vegetative and floral shoot apices, and the primordia of inflorescences.
4 citations
01 Jan 1988
TL;DR: In this paper, two-dimensional gels were run as previously described, and after electrophoresis the gels are silver stained with Bio-Rad reagents according to the procedure of Merril et al.
Abstract: wasassayedbythe Bradford method (3). Samples for two-dimensional elec-trophoresis were phenol-extracted (5). Depending on the organanalyzed, from 4 to 16 plants were used for each ofthe assaysdescribed above. Two-dimensional gels were run as previouslydescribed (2). After electrophoresis the gels were silver stainedwith Bio-Rad reagents according to the procedure ofMerril etal.
2 citations
Journal Article•
TL;DR: Quantitation of stained, electroeluted proteins by the classical Lowry and Bradford protein assay is not possible because of some different interferences, but these problems can be overcome by concentration and dialysis of electroeluting samples which permit the removal of interfering substances.
Abstract: Quantitation of stained, electroeluted proteins by the classical Lowry and Bradford protein assay is not possible because of some different interferences. In particular we have found that the substance interfering in the Lowry method cannot be removed by trichloroacetic acid precipitation nor can be compensated for by the appropriate blank. Interferences in the Bradford protein assay are due to detergents and pH of the protein buffer as well as to Coomassie brilliant blue R250 electroeluted with the protein sample. However, while these interferences can be compensated for by appropriate blank and standard curves, others (probably due to acrylamide fines) cannot be corrected. All these problems can be overcome by concentration and dialysis of electroeluted samples which permit the removal of interfering substances and the use of Bradford and Lowry protein assay in the 1-20 micrograms range, respectively. Successful applications are described for electroeluted bovine serum albumin, human hexokinase and phosphoglucomutase.
1 citations