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Glycosylated forms of nuclear lamins
Author(s) -
Ferrare A.,
Eufemi M.,
Cervoni L.,
Marinetti R.,
Turano C.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81543-1
Subject(s) - lamin , nuclear lamina , glycosylation , chromatin , phosphorylation , chemistry , concanavalin a , biochemistry , glycoprotein , methylation , nuclear protein , microbiology and biotechnology , biology , dna , transcription factor , in vitro , gene
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.