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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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Cytoplasmic serine hydroxymethyltransferase mediates competition between folate-dependent deoxyribonucleotide and S-adenosylmethionine biosyntheses.

TL;DR: Results indicate that cSHMT is a metabolic switch that, when activated, gives dTMP synthesis higher metabolic priority than SAM synthesis.
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A single amino acid substitution in rhodopsin (lysine 248----leucine) prevents activation of transducin.

TL;DR: Three mutants in the cytoplasmic loop between the putative transmembrane helices E and F are prepared by in vitro site-specific mutagenesis on bovine rhodopsin to stimulate the GTPase activity of transducin in a light-dependent manner.
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An introduction to methods for analyzing thiols and disulfides: Reactions, reagents, and practical considerations

TL;DR: In thiol–disulfide exchange reactions, it is important to consider reaction rate and the equilibrium constants between various thiol and disulfide species, because the thiolate anion is the reactive species, these properties are particularly sensitive to thiol pKa values.
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Changes in Lipid Peroxidation and Lipolytic and Free-Radical Scavenging Enzyme Activities during Aging and Sprouting of Potato (Solanum tuberosum) Seed-Tubers.

TL;DR: Results suggest that a gradual build-up of FRs leads to peroxidative damage of membrane lipids during aging of potato seed-tubers.
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Purification of insulin receptor with full binding activity.

TL;DR: In comparison, the receptor eluted from insulin-Sepharose with previously used conditions in the presence of urea resulted in maximum insulin binding of only 6 micrograms per mg of protein, indicating that a 4-to 5-fold increase in specific activity can be obtained by using the new elution conditions.
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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