ArticleBiochemistry research international2019
Protein Binding Characteristics of the Principal Green Tea Catechins: A QCM Study Comparing Crude Extract to Pure EGCG.
Article in Biochemistry research international, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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1 citing paper in PubMed, 5 citations in OpenAlex.
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5 authors at 2 institutions in 1 country.
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Abstract
Label-free detection methods such as the quartz crystal microbalance (QCM) are well suited to the analysis of molecular interactions in complex mixtures such as crude botanical extracts. In the present study, the binding characteristics of epigallocatechin gallate (EGCG) and crude green tea extract solutions to bovine serum albumin (BSA) have been investigated. The adsorbed mass levels onto BSA-functionalized surfaces were measured at various solution concentrations. Langmuir and Freundlich isotherms were used to model the adsorption data. The Langmuir isotherm better described the adsorption behavior with correlations of 0.68 and 0.70 for the EGCG and the crude extract solutions, respectively. The better fit of the Langmuir model indicates that adsorption occurs homogeneously and that aggregation is negligible. The mass saturation is estimated to be 58% higher for the crude green tea solution as compared to the pure EGCG solution (7.9 ng/cm
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