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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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Journal ArticleDOI

Decameric GTP cyclohydrolase I forms complexes with two pentameric GTP cyclohydrolase I feedback regulatory proteins in the presence of phenylalanine or of a combination of tetrahydrobiopterin and GTP.

TL;DR: Observations support the model that one molecule of GFRP binds to each of the two outer faces of the torus-shaped GTP cyclohydrolase I, and suggest that the complex has a radius of gyration similar to that of the enzyme itself.
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Calmodulin affinity chromatography yields a functional purified erythrocyte (Ca+ + Mg2+)-dependent adenosine triphosphatase.

TL;DR: The purification method is suitable for studying the lipid-sensitivity of the ATPase, since the lipids can easily be exchanged without a significant loss of activity.
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Uroporphyrinogen decarboxylase. Purification, properties, and inhibition by polychlorinated biphenyl isomers.

TL;DR: A new and simple method for the separation of free uroporphyrin, hepta-, hexa-, and pentacarboxylic porphyrins and coproporphirin was developed using a high pressure liquid chromatograph equipped with a spectrofluorometric detector.
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Purification and characterization of cholesterol 7 alpha-hydroxylase from rat liver microsomes.

TL;DR: The purified enzyme was purified from liver microsomes of cholestryramine-fed male rats by using high-performance ion-exchange chromatography and showed a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and its dithionite-reduced CO complex exhibited an absorption maximum at 450 nm.
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Purification and properties of phosphatidic acid phosphatase from porcine thymus membranes.

TL;DR: Although the enzyme appeared to be an integral membrane protein, the authors could not detect its phospholipid dependencies and it was judged to be specific to phosphatidic acid, since excess amounts of dicetylphosphate or lysophosphatodic acid did not inhibit the enzyme activity.
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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