Purification of a novel, nucleoplasmin-like protein from somatic nuclei.
AUTOR(ES)
Cotten, M
RESUMO
We have purified a nucleoplasmin-like protein from the nuclei of somatic Xenopus laevis cells. This protein possesses a number of the distinctive features of nucleoplasmin isolated from oocytes or unfertilized eggs. The protein is recognized by both monoclonal and polyclonal antisera raised against egg nucleoplasmin. The protein has an oligomeric structure, which must be heated in SDS to completely dissociate, is acidic, phosphorylated and efficiently promotes the in vitro formation of chromatin. We have partially characterized this novel protein and because of its resemblance to nucleoplasmin isolated from oocytes or unfertilized eggs we have named this protein nucleoplasmin S.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=553873Documentos Relacionados
- Z-DNA binding protein from chicken blood nuclei.
- A DNA-activated protein kinase from HeLa cell nuclei.
- Transcriptional activation of Xenopus class III genes in chromatin isolated from sperm and somatic nuclei.
- A novel 40S multi-snRNP complex isolated from rat liver nuclei.
- Protein Kinases in Soybean Nuclei.
