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

Reversible binding interactions between

Reversible binding interactions between the tryptophan enantiomers and albumins of different animal species as determined by novel high performance liquid chromatographic methods: an attempt to localize the D- and L-tryptophan binding sites on the human serum albumin polypeptide chain by using protein fragments

✍ Ladislav Šoltés; Bernard Sebille 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 172 KB 👁 2 views

The stereoselectivity of the reversible binding interactions between the Dand L-tryptophan enantiomers and serum albumins of different animal species and fragments of human serum albumin (HSA) was investigated by applying three novel high performance liquid chromatographic (HPLC) arrangements. The s