SDS-resistant Active and Thermostable Dimers Are Obtained from the Dissociation of Homotetrameric b-glycosidase From Hyperthermophilic Sulfolobus Solfataricus in SDS. Stabilizing Role of the A-C Intermonomeric Interface

Autor: Gentile F., Amodeo P., Febbraio F., Picaro F., Motta A. Formisano S., Nucci R.

Publikováno v: The Journal of biological chemistry
277 (2002): 44050–44060. doi:10.1074/jbc.M206761200
info:cnr-pdr/source/autori:Gentile F., Amodeo P., Febbraio F., Picaro F., Motta A. Formisano S., Nucci R./titolo:SDS-resistant Active and Thermostable Dimers Are Obtained from the Dissociation of Homotetrameric b-glycosidase From Hyperthermophilic Sulfolobus Solfataricus in SDS. Stabilizing Role of the A-C Intermonomeric Interface/doi:10.1074%2Fjbc.M206761200/rivista:The Journal of biological chemistry (Print)/anno:2002/pagina_da:44050/pagina_a:44060/intervallo_pagine:44050–44060/volume:277

beta-Glycosidases are fundamental, widely conserved enzymes. Those from hyperthermophiles exhibit unusual stabilities toward various perturbants. Previous work with homotetrameric beta-glycosidase from hyperthermophilic Sulfolobus solfataricus (M(r)

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http://www.cnr.it/prodotto/i/14953