Showing papers on "Bradford protein assay published in 2000"
TL;DR: The mechanism of eosin binding to proteins, which varies with solution pH so that a wide range of protein concentrations can be estimated, is described and the reason for the higher absorbance of protein-eosin Y complex compared to that ofprotein-eOSin B complex is discussed.
90 citations
TL;DR: In this paper, the resonance Rayleigh scattering (RRS) spectrum of 4-azochromotropic acid phenylfluorone has a peak at 337nm, and the RRS intensity is enhanced by small amounts of protein due to the binding interaction of protein and the dye.
60 citations
TL;DR: The results highlight that the estimation of protein can be affected by methodology and by sample composition, and shows that methods must be optimized for a particular application.
40 citations
TL;DR: In this article, a new method is described for the spectrophotometric determination of protein based on the binding interaction of protein, molybdenum(VI) and dibromohydroxyphenylfluorone (DBHPF).
27 citations
TL;DR: In this paper, a protein assay with the determination sensitivity at nanogram levels has been developed based on measurement of enhanced resonance light scattering (RLS) in a neutral aqueous medium, the interactions of ABGX with different proteins were found to result in strongly enhanced RLS signals.
Abstract: A protein assay with the determination sensitivity at nanogram levels has been developed based on measurement of enhanced resonance light scattering (RLS). In a neutral aqueous medium, the interactions of ABGX with different proteins were found to result in strongly enhanced RLS signals. With the enhanced RLS signals at 398.0 nm, proteins, including bovine serum albumin (BSA), human serum albumin (HAS), pepsin (Pep) and cellulase (Cel), can be determined with the limit of detection below 30 ng/ml. The results of determinations for artificial samples were in agreement with the desired values, and those for human serum samples were identical with those obtained according to the Bradford method using CBB G-250.
24 citations
TL;DR: A protein redistribution assay that combines reversible metal chelate-based total protein detection with a four-fraction subcellular detergent fractionation procedure is reported on, revealing a new level of complexity regarding NFkappaB distribution and translocation.
14 citations
TL;DR: A rapid, continuous assay in which brain PLA(2) activity is measured in a continuous, rapid, and sensitive manner in mouse brain cytosol is described.
7 citations
Journal Article•
TL;DR: The analytical performance of a new assay for plasma lipoprotein(a)-cholesterol (Lp[a]-C) was compared with that of the existing Lp(a) protein assay and it is concluded that the Lp (a)-C assay system performs well but that further information is required.
Abstract: The analytical performance of a new assay for plasma lipoprotein(a)-cholesterol (Lp[a]-C) was compared with that of our existing Lp(a) protein assay. The Lp(a)-C assay utilises lectin affinity chromatography to isolate intact Lp(a) particles. The effect of apo(a) isoform size on this system was assessed and found to be negligible. Plasma Lp(a) concentrations measured by both assays were in excellent accord in 24 subjects with Lp(a) protein concentrations ranging from 1-65 mg/dL (r2 = 0.916). Linearity of the Lp(a)-C assay system was excellent (r2 = 0.997) and within-run precision was 6.9% at an Lp(a)-C concentration of 0.3 mmol/L. Between-calibration precision was checked and proved to be 7.9%. The lectin-binding reagent used in the assay bound different sized apo(a) isoforms equally, and the recovery of Lp(a) from the reagent was, on average, 64%. We conclude that the Lp(a)-C assay system performs well but that further information is required on what new information, if any, the assay provides over traditional Lp(a) protein measurements by enzyme-linked immunosorbent assay (ELISA) or immunoturbidimetry.
5 citations