ArticleAnalytical biochemistry2015
Evaluation of colorimetric assays for analyzing reductively methylated proteins: Biases and mechanistic insights.
Article in Analytical biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 54 citations in OpenAlex.
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- Determination of the protein content of complex samples by aromatic amino acid analysis, liquid chromatography-UV absorbance, and colorimetry.Analytical and bioanalytical chemistry · 2022Article
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- Lysate-based pipeline to characterize microtubule-associated proteins uncovers unique microtubule behaviours.Nature cell biology · 2022Article
- Comparative study of the most commonly used methods for total protein determination in milk of different species and their ultrafiltration products.Frontiers in nutrition · 2022Article
- Methyl-Induced Polarization Destabilizes the Noncovalent Interactions of N-Methylated Lysines.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
Colorimetric protein assays, such as the Coomassie blue G-250 dye-binding (Bradford) and bicinchoninic acid (BCA) assays, are commonly used to quantify protein concentration. The accuracy of these assays depends on the amino acid composition. Because of the extensive use of reductive methylation in the study of proteins and the importance of biological methylation, it is necessary to evaluate the impact of lysyl methylation on the Bradford and BCA assays. Unmodified and reductively methylated proteins were analyzed using the absorbance at 280 nm to standardize the concentrations. Using model compounds, we demonstrate that the dimethylation of lysyl ε-amines does not affect the proteins' molar extinction coefficients at 280 nm. For the Bradford assay, the responses (absorbance per unit concentration) of the unmodified and reductively methylated proteins were similar, with a slight decrease in the response upon methylation. For the BCA assay, the responses of the reductively methylated proteins were consistently higher, overestimating the concentrations of the methylated proteins. The enhanced color formation in the BCA assay may be due to the lower acid dissociation constants of the lysyl ε-dimethylamines compared with the unmodified ε-amine, favoring Cu(II) binding in biuret-like complexes. The implications for the analysis of biologically methylated samples are discussed.
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