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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

Purification and reconstitution of a Ca2+ pump from human platelets.

TL;DR: The platelet Ca2+ pump is similar to the ATPase from the sarcoplasmic reticulum in structure and function, and the Ca2-ATPase is a major membrane component in platelet membranes, and this emphasizes the importance ofCa2+ fluxes in Platelet function.
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Formation of a carboxyarabinitol bisphosphate complex with ribulose bisphosphate carboxylase/oxygenase and theoretical specific activity of the enzyme

TL;DR: Various enzyme preparations from spinach leaves tightly bound 2-carboxyarabinitol- P 2 in proportion to their specific activities, with a theoretical specific activity of 2.8 μmol · min −1 · mg protein −1 was indicated.
Journal ArticleDOI

Isoenzyme patterns in soybean-Nicotiana somatic hybrid cell lines

TL;DR: Variations in the zymogram of the cell lines were observed during a culture period of 8 months (more than 100 generations), and these variations may be related to chromosomal loss from the hybrid, particularly those of the Nicotiana parent.
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Steady state kinetics of ATP synthesis and hydrolysis catalyzed by reconstituted chloroplast coupling factor.

TL;DR: The steady state kinetics of ATP synthesis and hydrolysis catalyzed by the chloroplast dicyclohexylcarbodiimide-sensitive ATPase reconstituted into phospholipid vesicles were studied as a function of the transmembrane proton gradient.
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Catabolism of Ap3A and Ap4A in human plasma. Purification and characterization of a glycoprotein complex with 5'-nucleotide phosphodiesterase activity.

TL;DR: Optimal activity of the hydrolase was found at pH 8.5 and binding of the native enzyme to concanavalin-A--Sepharose and specific inhibition of binding by methyl mannoside indicated that thehydrolase is a glycoprotein.
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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