Topic
Bovine serum albumin
About: Bovine serum albumin is a(n) research topic. Over the lifetime, 19981 publication(s) have been published within this topic receiving 571291 citation(s). The topic is also known as: BSA.
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TL;DR: Under the new conditions there is direct proportionality between absorbance at 650 nm and weight of protein within the range 15–110 μg.
Abstract: 1. 1. The Lowry, Rosebrough, Farr, and Randall method for protein assay has been modified so as to give a higher color yield with bovine serum albumin and with five other pure proteins. 2. 2. Under the new conditions there is direct proportionality between absorbance at 650 nm and weight of protein within the range 15–110 μg.
5,067 citations
TL;DR: The results by this method agree very well with those obtained by electrophoresis and salt fractionation and the method is simple, it has excellent precision and the reagents are stable.
Abstract: A rapid and reliable method for measuring serum albumin employing bromcresol green is described. The addition of albumin to a solution of bromcresol green in a 0.075 M succinate buffer pH 4.20 results in an increase in absorbance at 628 nm. The absorbance-concentration relationship is linear for samples containing up to 6 g/dl albumin. Bilirubin, moderate lipemia, and salicylate do not interfere with the analysis. The use of nonionic surfactant (Brij-35) reduces the absorbance of the blank, prevents turbidity and provides linearity. The results by this method agree very well with those obtained by electrophoresis and salt fractionation. The method is simple, it has excellent precision and the reagents are stable. A protein standard is introduced which can be employed for both the total serum proteins and albumin determinations.
3,175 citations
TL;DR: The Lowry protein assay is a sensitive but highly nonspecific procedure that has been modified so that protein can be assayed in the presence of interfering chemicals.
Abstract: The Lowry protein assay is a sensitive but highly nonspecific procedure. The standard Lowry protein assay has been modified so that protein can be assayed in the presence of interfering chemicals. The method is based on the observation that in the presence of 125 μg/ml of Na-deoxycholate, bovine serum albumin (5—50 μg) is reproducibly precipitated (90–104%) by 6% trichloroacetic acid. Interference by sucrose, glycerol, Tris—HCl, Tricine, and EDTA can be eliminated. Protein samples containing carrier ampholytes can also be assayed provided their NaCl concentration is adjusted to 1 m .
3,099 citations
Journal Article•
TL;DR: Bacterial adsorbent not only had a distinct advantage in speed of antigen isolation, but analyses by polyacrylamide gel electrophoresis in SDS also revealed consistently higher antigen recoveries, lower levels of background radioactivity, and an absence of other cell components which may nonspecifically bind to and complicate analyses using conventional immune precipitates.
Abstract: The Cowan I strain of the bacterium Staphylococcus aureus has been used as an adsorbent for antibodies complexed with radiolabeled antigens from cell lysates. This application is advanced as a superior alternative to other methods of immune precipitation for the isolation of antigens. It exploits the high adsorption capacity for IgG molecules by protein A molecules on the cell walls of certain strains of staphylococci, along with the advantageous sedimentation properties of the bacteria. The interaction of immune complexes with the adsorbent was defined initially using a model system of bovine serum albumin with a high excess of rabbit anti-bovine serum albumin antibodies (IgG). The uptake of immune complexes under these conditions was extremely rapid, occurring within seconds, whereas maximum binding of free IgG was much slower. In addition, once bound the complexed antigen could not be displaced from the adsorbent either by large amounts of normal IgG or by extra free antibody. Antigen could be eluted almost completely from the inert adsorbent for analytic or preparative purposes with a variety of solvent systems, such as the detergent SDS in combination with urea and high temperature, and neutral salts with strong lyotropic salting in properties. The efficacy of the protein A-antibody adsorption technique was tested in direct comparisons with a conventional double antibody precipitation method for the isolation of mouse lymphocyte IgM. The bacterial adsorbent not only had a distinct advantage in speed of antigen isolation, but analyses by polyacrylamide gel electrophoresis in SDS also revealed consistently higher antigen recoveries, lower levels of background radioactivity, and an absence of other cell components which may nonspecifically bind to and complicate analyses using conventional immune precipitates.
2,760 citations
TL;DR: This protein assay is described in which the sample is precipitated with trichloroacetic acid in the presence of sodium dodecylsulfate, filtered off on a Millipore membrane and stained with Amidoschwarz 10B, and its absorbance determined at 630 nm.
Abstract: A protein assay is described in which the sample is precipitated with trichloroacetic acid in the presence of sodium dodecylsulfate, filtered off on a Millipore membrane and stained with Amidoschwarz 10B. The proteindye complex is eluted, and its absorbance determined at 630 nm. This assay is very reproducible, insensitive to variations in assay conditions, and linear from 3 to 30 μg of protein. It can be used on samples with a concentration as low as 0.75 μg/ml. There is no interference by commonly used reagents such as Tris, thiol reagents, EDTA, urea, sucrose, and many others. The color yield for a variety of proteins was determined and found to lie within ±15% of the value for bovine serum albumin which was used as standard. Of the proteins tested only insulin, which due to its low molecular weight was incompletely retained on the membrane in the filtration step, gave a low color yield, 50% of the standard.
2,429 citations