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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: An adaptation of the Lowry (1951) method has been developed for quantifying proteins in organic reversed micellar solutions with Ethanol added to improve the re-extraction of the proteins from the micelles.
Abstract: An adaptation of the Lowry (1951) method has been developed for quantifying proteins in organic reversed micellar solutions. Ethanol is added to improve the re-extraction of the proteins from the micelles and a centrifugation step is included to separate the organic phase.
11 citations
TL;DR: PLE-IA was applied in a study of follistatin, a 31.5 kDa glycoprotein regulating mammalian cell proliferation and differentiation and should find application in study of cell signaling, including questions related to aging and regeneration.
Abstract: We introduce a fully integrated multistep protein assay that reports both protein identity and size. To report these two properties, a microfluidic design strategy integrates pore limit electrophoresis (PLE) with a heterogeneous immunoassay in a single microchannel (PLE-IA). PLE-IA was applied in a study of follistatin, a 31.5 kDa glycoprotein regulating mammalian cell proliferation and differentiation. In a single-channel multistage assay approach, an antibody to follistatin was first immobilized in a polyacrylamide PLE gradient gel, near the origin of the separation axis. Immobilization relies on pore-limit exclusion of the antibody and not on chemical functionalization of either the sieving matrix or the antibody, making assay customization by an end-user straightforward. Subsequently, target and ladder protein species were electrophoretically introduced into the antibody-patterned PLE channel. Species having an affinity for the immobilized antibody were detected via heterogeneous immunoassay. Noninter...
11 citations
TL;DR: The assay is based on the transformation of hematoxylin to its two-electron-oxidized product, hematein, which has an absorption maximum and extinction coefficient similar to those of the commonly used O 2 – scavenger, cytochrome c .
Abstract: Publisher Summary This chapter discusses the assays for superoxide dismutase (SOD) based on the autoxidation of hematoxylin. The assay is based on the transformation of hematoxylin to its two-electron-oxidized product, hematein. The assay is sensitive and simple. The reaction product, hemarein, is relatively stable and has an absorption maximum and extinction coefficient similar to those of the commonly used O 2 – scavenger, cytochrome c . The reaction is inhibited by SOD and can be performed in the physiological pH range of 6.8–7.8, where SOD inhibits the reaction 90–95%. In addition, at pH values above 8.1, the autoxidation reaction is accelerated by added SOD, and the reaction becomes a positive assay for the enzyme, similar in principle to SOD assays based on the photochemical and enzymatic oxidation of dianisidine. The activity of purified SOD is determined by the xanthine oxidase cytochrome c method. Xanthine oxidase is isolated from unpasteurized cream. General protein is determined by the Bradford assay using bovine serum albumin (BSA) as a standard.
11 citations
TL;DR: Use of this procedure offers the advantage of allowing liquid scintillation counting in toluene and protein assay on aliquots of the same sample, and it is suggested to be a good procedure for measurement of protein concentration in Hyamine hydroxide or NCS solution.
11 citations
TL;DR: It was found that both Bradford and Lowry methods are not suitable for the protein assay in the HPCH sample, and the BCA method could be used to determine protein content in HPCH solutions at low concentrations with good accuracy and precision.
11 citations