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The antioxidant activity of alpha-tocopherol-bovine serum albumin complex in micellar and liposome autoxidations.

1985; Elsevier BV; Volume: 260; Issue: 29 Linguagem: Inglês

10.1016/s0021-9258(17)36330-5

1083-351X

L. R. C. Barclay, A. Bailey, Dedong Kong,

Protein Interaction Studies and Fluorescence Analysis

A comparison is made of the antioxidant activity of a water-soluble form of alpha-tocopherol complexed with bovine serum albumin (alpha-T X BSA) with that of micellar alpha-tocopherol and aqueous 6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylate (Trolox) to inhibit autoxidation of linoleic acid in sodium dodecyl sulfate micelles. The peroxyl radical trapping ability of alpha-T X BSA compares favorably with that of alpha-tocopherol and Trolox, and all three can be used in quantitative measurements of the susceptibility of the micellar substrate to undergo autoxidation: the oxidizability, for reactions initiated in the micellar phase by di-tertbutylhyponitrite (DBHN) or in the aqueous phase by azobisamidinopropane hydrochloride (ABAP). alpha-Tocopherol and Trolox are also effective antioxidants to inhibit DBHN- or ABAP-initiated autoxidations of dilinoleoylphosphatidylcholine (DLPC) liposomes prepared as multilamellar or unilamellar bilayers characterized by 31P NMR spectra. The oxidizability of DLPC liposomes is determined by various combinations of water-soluble and lipid-soluble initiators and the antioxidants, alpha-tocopherol and Trolox. In contrast, alpha-T X BSA does not effectively trap peroxyl radicals when it is added after initiation of autoxidation in the lipid phase (DBHN) or in the aqueous phase (ABAP). The radical trapping ability of alpha-T X BSA becomes evident if it is mixed with the DLPC for some hours before initiation. This result is interpreted in terms of diffusion of alpha-tocopherol from the bound alpha-T X BSA form to the liposome before it exhibits antioxidant activity.