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Nucleic Acids Res ; 17(5): 1845-63, 1989 Mar 11.
Article in English | MEDLINE | ID: mdl-2928110

ABSTRACT

HeLa cell OTF-1 has been purified on the basis of its DNA binding activity and used to raise a polyclonal rabbit antiserum. This antiserum is shown to recognize both native and denatured OTF-1 from both human and a similar protein from Xenopus culture cells, but to react either more weakly or not at all with the lymphoid cell-specific OTF-2. Separately, NFIII has been purified on the basis of its ability to stimulate Adenovirus DNA replication in vitro. On denaturing polyacrylamide gels OTF-1 and NFIII exhibit identical mobility. Anti-OTF-1 antiserum recognizes NFIII and neutralizes its stimulatory effect on DNA replication. Moreover, OTF-1 can functionally replace NFIII. Taken together with previously published DNA binding data, this indicates that OTF-1 and NFIII are either very closely related or identical.


Subject(s)
Adenoviruses, Human/genetics , Antibodies/physiology , DNA, Viral/biosynthesis , Nuclear Proteins/physiology , Transcription Factors/immunology , Animals , Antigen-Antibody Reactions , Binding, Competitive , HeLa Cells , Humans , Immune Sera/pharmacology , Nuclear Proteins/immunology , Nuclear Proteins/isolation & purification , Transcription Factors/isolation & purification , Xenopus
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