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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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Phenobarbital-induced rat liver cytochrome P-450. Purification and characterization of two closely related isozymic forms.

TL;DR: This present demonstration of closely related isozymic forms of phenobarbital-induced cytochrome P-450 species suggests the possible added complexity of microheterogeneity for this family of microsomal monooxygenases.
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Proteome research: Complementarity and limitations with respect to the RNA and DNA worlds

TL;DR: Proteome analysis is demonstrated as being capable of proceeding independently of DNA sequence information and aiding in genomic annotation, and a challenge for proteome analysis into the future will be to reduce its dependence on two‐dimensional gel electrophoresis as the preferred method of separating complex mixtures of cellular proteins.
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Catalytic activity of cytochrome P-450 isozyme 3a isolated from liver microsomes of ethanol-treated rabbits. Oxidation of alcohols.

TL;DR: Isozyme 3a catalyzes the oxidation of methanol, 1-propanol, and 1-butanol as well as ethanol; the relationships between the apparent Km values for these alcohols and their octanol-water partition coefficients is in accord with the known hydrophobic nature of the P-450 binding site.
Journal ArticleDOI

Purification of the glucocorticoid receptor from rat liver cytosol.

TL;DR: The [3H]-triamcinolone acetonide-labeled glucocorticoid receptor from rat liver cytosol was purified to 85% homogeneity according to sodium dodecyl sulfate gel electrophoresis as discussed by the authors.
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Isolation and characterization of cancer procoagulant: a cysteine proteinase from malignant tissue.

Anna Falanga, +1 more
- 24 Sep 1985 - 
TL;DR: The proteinase activity of cancer procoagulant directly activated factor X, in the absence of factor VII, and was inhibited by 1 mM iodoacetamide and 0.1 mM mercury which are classic cysteine proteinase inhibitors.
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.
Journal ArticleDOI

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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