title: Glycosylated forms of nuclear lamins.
abstract: Chromatin and pore complex-lamina preparations were obtained from pig and chicken tissues, and their proteins were analysed by mono- and bidimensional electrophoresis. A glycosylated form of lamin A, recognized by concanavalin A, was shown to be present in at least 3 of the tissues examined. Glycosylation is suggested to be a further postsynthetic modification, besides phosphorylation and methylation, which can modify the properties of lamins.
authors.affiliation: Department of Biochemical Sciences, University of Rome, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Ferraro
authors.forename: M
authors.initials: M
authors.lastname: Eufemi
authors.forename: L
authors.initials: L
authors.lastname: Cervoni
authors.forename: R
authors.initials: R
authors.lastname: Marinetti
authors.forename: C
authors.initials: C
authors.lastname: Turano
mesh_terms: D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism*; D002645:Chickens; D002843:Chromatin / Q000378:metabolism; D003208:Concanavalin A / Q000378:metabolism; D015180:Electrophoresis, Gel, Two-Dimensional; D006031:Glycosylation; D034904:Lamin Type A; D034882:Lamins; D008970:Molecular Weight; D009687:Nuclear Proteins / Q000378:metabolism*; D013552:Swine
chemical_list: D002843:Chromatin; D034904:Lamin Type A; D034882:Lamins; D009687:Nuclear Proteins; D003208:Concanavalin A