ArticleOpen biology2024
Evaluating the efficacy of protein quantification methods on membrane proteins.
Article in Open biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed.
- Comparative analysis of freeze-drying and spray-drying on the physicochemical modulation and symbiotic functionality of egg white forFood chemistry: X · 2026Article
- Metabolic Marker GLUT1 in Salivary Gland Cancers: Quantification and Effect-Size Estimation.Biomedicines · 2026Article
- A Novel Role for the Small Molecule Cinnamaldehyde in Protecting AgainstAntioxidants (Basel, Switzerland) · 2026Article
- Freezing diluted bovine serum albumin standards does not significantly affect standard curves.BioTechniques · 2025Article
- Article
- Evaluation of cosmetic efficacy of lychee seed fermentation liquid.Bioresources and bioprocessing · 2024Article
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Abstract
Protein quantification is an important tool for a wide range of biological applications. The most common methods include the Lowry, bicinchoninic acid (BCA) and Coomassie Bradford assays. Despite their wide applicability, the mechanisms of action imply that these methods may not be ideal for large transmembrane proteins due to the proteins' integration in the plasma membrane. Here, we investigate this problem by assessing the efficacy and applicability of these three common protein quantification methods on a candidate transmembrane protein: Na, K-ATPase (NKA). We compared these methods with an ELISA, which we newly developed and describe here for the quantification of NKA. The use of a relative standard curve allows this ELISA to be easily adapted to other proteins and across the animal kingdom. Our results revealed that the three conventional methods significantly overestimate the concentration of NKA compared with the ELISA. This is due to the samples containing a heterogeneous mix of proteins, including a significant amount of non-target proteins. Further, by applying the protein concentrations determined by the different methods to
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