Water-Soluble Complexes Formed by Natural Polyphenols and Bovine Serum Albumin: Evidence from Gel Electrophoresis

Human Serum Albumin as an Antioxidant in the Oxidation of (−)-Epigallocatechin Gallate: Participation of Reversible Covalent Binding for Interaction and Stabilization

“…Binding affinity of pyrogallol-type catechins with HSA in aqueous solutions Several analytical approaches, including electrophoresis, spectrofluorometry, and chromatography, have indicated that catechins noncovalently bind to serum albumin. [22][23][24] HPLC with an HSA column recently enabled us to show that the hydroxyl groups on the galloyl group of each catechin influenced the binding affinity for immobilized HSA in an acidic solution with 20% acetonitrile. 25) We investigated in a QCM in the present study the interaction between pyrogallol-type catechins (EGC and EGCg) and HSA immobilized under physiological conditions.…”

Epigallocatechin Gallate Inactivates Clinical Isolates of Herpes Simplex Virus

“…A mixture of EGCG (250 g/ml) and BSA, gB, or gD (500 to 700 g/ml) in a 0.1 M K 2 HPO 4 -KH 2 PO 4 buffer (pH 7.0) was incubated at 35°C in a water bath for 24 h, and the products were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) (22). Ten microliters of each product was mixed with an equal volume of sample buffer and denatured at 50°C for 15 min.…”

Interaction of Polyphenols with Proteins: Binding of (-)-Epigallocatechin Gallate to Serum Albumin, Estimated by Induced Circular Dichroism

“…7,8) Size exclusion chromatography (SEC) and polyacrylamide gel electrophoresis (PAGE) are valuable tools for observing the formation of such large complexes. However, although these methods are adequate for observing large differences in the molecular sizes of the complexes, the formation of these complexes requires several hours.…”