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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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Protein extraction from Phoenix dactylifera L. leaves, a recalcitrant material, for two- dimensional electrophoresis

TL;DR: DOC with TCA/acetone precipitation step eliminates interfering compounds, thus allowing efficient resolubilization of date palm leaf proteins, which could be appropriate for proteomic studies such as date palm colonization by entomopathogenic fungi.
Journal ArticleDOI

Collagenase Production by Nematode-Trapping Fungi

TL;DR: Collagenase, which is active on ichthyocol, earthworm collagen, and procollagen from chicken embryo fibroblasts, was found in the growth medium of all tested species; keratinase was not found and may aid the fungus to penetrate the cuticle of its prey.
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Apolipoprotein E quantified by enzyme-linked immunosorbent assay.

TL;DR: In this paper, a Sandwich-type enzyme-linked immunosorbent (SILI) assay was developed to quantify apolipoprotein E in serum and in its lipoprotein fractions.
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Incorporation of methylamine in an ultrasensitive silver stain for detecting protein in thick polyacrylamide gels

TL;DR: An ultrasensitive silver stain is described for the detection of proteins in 4–20 % w/v polyacrylamide gradient gels of 3mm thickness and the sensitivity was at least equal to that of the newly described photochemical technique.
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Cloning and expression of the gene encoding the soluble cytochrome b562 of Escherichia coli

TL;DR: It is demonstrated that the genomic sequence codes for a classic N-terminal signal sequence and that mature cytochrome b562 is translocated to the periplasmic space.
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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