Glycosylated forms of nuclear lamins.
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.
Ferraro
A
A
Department of Biochemical Sciences, University of Rome, Italy.
Eufemi
M
M
Cervoni
L
L
Marinetti
R
R
Turano
C
C
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
D002843:Chromatin; D034904:Lamin Type A; D034882:Lamins; D009687:Nuclear Proteins; D003208:Concanavalin A