Autor: |
Lapshina MA; Molecular Biology Laboratory, Institute of Problems of Chemical Physics RAS, Chernogolovka, Moscow Region, 142432, Russia. lapshina@icp.ac.ru, Parkhomenko II, Terentiev AA |
Jazyk: |
angličtina |
Zdroj: |
Annals of the New York Academy of Sciences [Ann N Y Acad Sci] 2006 Dec; Vol. 1090, pp. 177-81. |
DOI: |
10.1196/annals.1378.019 |
Abstrakt: |
Like many other transcription factors, the tumor suppressor protein p53 is bound to the nuclear matrix (NM). To study the interaction of p53 with the NM in more detail, we used alkaline and acidic extractions of NM proteins. It was found that there are two forms of p53, alkali- and acid-soluble, in NM of HEK293 cells and only one alkali-soluble form in NM of actinomycin D-treated MCF-7 cells. We suggest that distinct forms of p53 differ either in interactions with NM proteins or in their charges. |
Databáze: |
MEDLINE |
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