Abstract
Abstract Bradford protein-binding dye, Coomassie brilliant blue G-250, formed intensively blue-colored complexes with hydrolyzable tannins. The tannin–dye aggregates displayed a broad absorption maximum around 700 nm, with a shoulder at 620 nm. Pronounced reactivities were observed with tetra- to nonagalloylglucoses. Gallic acid, β-glucogallin and digalloylglucose were inactive and trigalloylglucose gave only a weak reaction. Moderate color formation (65% relative to pentagalloylglucose) was observed for the ellagitannin, tellimagrandin II. Monomeric and dimeric proanthocyanidins gave only traces of color. These complexation characteristics parallel the binding of hydrolyzable tannins to proteins.
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