Purification of a novel, nucleoplasmin-like protein from somatic nuclei.
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.
Department of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN 37232.
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Cotten
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Chalkley
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002460:Cell Line; D002467:Cell Nucleus / Q000032:analysis*; D002843:Chromatin / Q000648:ultrastructure; D007668:Kidney; D009687:Nuclear Proteins / Q000302:isolation & purification* / Q000378:metabolism; D056489:Nucleoplasmins; D010750:Phosphoproteins; D014982:Xenopus laevis
D000596:Amino Acids; D002843:Chromatin; D009687:Nuclear Proteins; D056489:Nucleoplasmins; D010750:Phosphoproteins