title: Site selectivity in the glycation of alpha A- and alpha B-crystallins by glucose.
abstract: We determined the site selectivity of glycation by glucose (glucosylation) in alpha A- and alpha B-crystallins using two independent approaches. HPLC purified 14C-glucose labeled chymotryptic peptides and affinity chromatography/HPLC purified fully glycated peptides were identified by FAB-MS. Lys 11 and 78 of alpha A-crystallin and Lys 90 and/or 92 of alpha B-crystallin were the fast reacting sites of glucosylation.
authors.affiliation: Department of Biochemistry and Molecular Biology, Medical College of Georgia, Augusta 30912.
authors.forename: E C
authors.initials: EC
authors.lastname: Abraham
authors.forename: M
authors.initials: M
authors.lastname: Cherian
authors.forename: J B
authors.initials: JB
authors.lastname: Smith
mesh_terms: D000818:Animals; D002417:Cattle; D018833:Chaperonins; D002851:Chromatography, High Pressure Liquid; D003459:Crystallins / Q000737:chemistry*; D008401:Gas Chromatography-Mass Spectrometry; D005947:Glucose / Q000737:chemistry*; D017127:Glycation End Products, Advanced; D066298:In Vitro Techniques; D008239:Lysine / Q000737:chemistry; D010449:Peptide Mapping; D011506:Proteins / Q000737:chemistry
chemical_list: D003459:Crystallins; D017127:Glycation End Products, Advanced; D011506:Proteins; D018833:Chaperonins; D005947:Glucose; D008239:Lysine