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Assay of proteins in the presence of interfering materials.

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TLDR
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.
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This article is published in Analytical Biochemistry.The article was published on 1976-01-01. It has received 3135 citations till now. The article focuses on the topics: Lowry protein assay & Bicinchoninic acid assay.

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Citations
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Glucose oxidase overproducing and negative mutants of Aspergillus niger

TL;DR: It can be concuded that oxygen- and carbonsource-dependent induction are mediated by different factors in Aspergillus niger which showed altered glucose oxidase induction.
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The ABC transporter BmrA from Bacillus subtilis is a functional dimer when in a detergent-solubilized state

TL;DR: Sedimentation-velocity and equilibrium experiments unequivocally supported that BmrA purified in DDM is a dimer and excluded the presence of other oligomeric states, an important first step towards crystallographic studies of BMRA structure.

Original article Characterisation of protein-rich isolates and antioxidative phenolic extracts from pale and black brewers' spent grain

TL;DR: The protein-enriched isolates and the phenolic-rich extracts may find use as value-added ingredients for incorporation into conventional and functional foods and the presence of phenolics, with higher concentrations in the black BSG extracts is revealed.
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Antioxidant system in Boea hygroscopica: Changes in response to desiccation and rehydration

TL;DR: In leaves of Boea hygroscopica subjected to either rapid or slow dehydration and rehydration, the response to H 2 O 2 production was studied by monitoring the changes in the amount of ascorbic and dehydroascorbic acids as well as the amounts of reduced and oxidized glutathione and related enzyme activities.
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Interaction of F1-ATPase, from ox heart mitochondria with its naturally occurring inhibitor protein. Studies using radio-iodinated inhibitor protein.

TL;DR: The results suggest the presence of a single, high-affinity, inhibitory binding site for inhibitor protein on membrane-bound F1, and suggest that a delocalised energy pool is important in promoting inhibitor protein release from F1.
References
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Journal Article

Protein Measurement with the Folin Phenol Reagent

TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
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Interference by detergents, chelating agents, and buffers with the Lowry protein determination.

TL;DR: The effect of succinic acid, sodium citrate, and Bicine on the Lowry method changes depending on the concentration of the chemicals, but the changes were not as significant as in the case of the chemical mentioned above.
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Interferences by sulfhydryl, disulfide reagents and potassium ions on protein determination by Lowry's method.

TL;DR: The concentrations ofulfhydryl, disulfide reagents, and also potassium ions interfere with the protein determination by Lowry's method, but at moderate concentrations this interference can be overcome by running appropriate blanks.
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