title: Effect of galactose on alpha-crystallin.
abstract: Chromatographic separation of alpha-crystallin incubated with [3H]-labelled galactose showed the radioactivity to be concentrated in the low molecular mass subunits (20 and 40 kDa). The effect of glycation on the structural organization of alpha-crystallin was evaluated by FPLC analysis of native (pH 6.8 and 8.2) and glycated protein in dissociating conditions. Results suggest that the glycation acts on the protein surface by altering its charge distribution.
authors.affiliation: Istituto Mario Negri, Consorzio Mario Negri Sud, S. Maria Imbaro, Chieti, Italy.
authors.forename: F
authors.initials: F
authors.lastname: Facchiano
authors.forename: T
authors.initials: T
authors.lastname: Libondi
authors.forename: P
authors.initials: P
authors.lastname: Stiuso
authors.forename: C
authors.initials: C
authors.lastname: Esposito
authors.forename: R
authors.initials: R
authors.lastname: Ragone
authors.forename: G
authors.initials: G
authors.lastname: Colonna
mesh_terms: D000818:Animals; D002417:Cattle; D002853:Chromatography, Liquid; D003432:Cross-Linking Reagents; D003459:Crystallins / Q000737:chemistry*; D005690:Galactose / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D011485:Protein Binding
chemical_list: D003432:Cross-Linking Reagents; D003459:Crystallins; D005690:Galactose