Antioxidant properties of ?-crystallin

Manzanares D.; Bauby, C; de la Pena, R; Garcia J.C.; Sanchez R.; Martínez, S.; Romay Ch.; Lopez-Reconde J.L.; Pino E.; Lissi E.A.

Keywords: acid, oxygen, antioxidants, animals, serum, brain, protein, cell, structure, stress, alpha, family, ultraviolet, antioxidant, humans, radiation, subunit, cattle, interaction, metabolite, crystallins, radical, albumin, radicals, neutrophils, hypochlorite, article, substances, lens, autooxidation, crystalline, peroxides, neutrophil, chaperone, measurements, phycocyanin, oxidative, Free, Reactive, luminol, chemoluminescence, Chemiluminescent, Bovinae, Oxidation-Reduction, crystallin, thiobarbituric, homogenate, zymosan, peroxy, Hypochlorous, Lens,, polymorphonuclear


?-Crystallin is a major chaperone lens protein to which has been ascribed antioxidant functions. In the present work we have evaluated the antioxidant and free radical scavenging properties of bovine ?-crystallin in a series of in vitro models: zimosan-induced, luminol-enhanced chemiluminescence response of polymorphonuclear leukocytes, the autoxidation of brain homogenate, bleaching of 2,2?-azinobis(3-ethylbenzothiazoline-6- sulfonic acid)-derived radical cations, trapping of peroxyl radicals, and reactivity toward hypochloric acid. In all these systems, the reactivity of ?-crystallin is higher than or similar to that of bovine serum albumin. It is concluded that, given the high concentrations of ?-crystallin in the lenses, its capacity to interact with free radicals and to remove hypochlorous acid could contribute to the maintenance of the lens functionality. © 2001 Plenum Publishing Corporation.

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Título según SCOPUS: Antioxidant properties of ?-crystallin
Título de la Revista: PROTEIN JOURNAL
Volumen: 20
Número: 3
Editorial: Springer
Fecha de publicación: 2001
Página de inicio: 181
Página final: 189
Idioma: English