In vitro oxidation of intrinsic sulfhydryl groups yields polymers of the two predominant polypeptides in the nuclear envelope fraction.
The two quantitatively predominant nuclear nonhistone polypeptides of the avian erythrocyte comprise a significant portion of the nuclear envelope protein. Each of these two polypeptides can be converted almost completely to homogeneous polymeric species via oxidation of intrinsic sulfhydryl groups by omicron-phenanthroline cupric ion complex. Major products are two dimeric species arising from each of the approximately 77 000-dalton pair. The larger of the two polypeptides also yields oligomers greater than dimers. These observations extend out earlier solubility and polypeptide cross-linking evidence which indicated that these polypeptides were involved in an oligomeric, proteinaceous nuclear structure. Ultramicroscopic studies from other laboratories indicate that such a structure may function as a nuclear skeleton. The architectural details of the structure now appear to be accessible at the molecular level.
D000818:Animals; D002467:Cell Nucleus / Q000032:analysis*; D002645:Chickens / Q000097:blood; D004220:Disulfides / Q000032:analysis; D004912:Erythrocytes / Q000032:analysis; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000097:blood; D008970:Molecular Weight; D009685:Nuclear Envelope / Q000032:analysis*; D010084:Oxidation-Reduction
D004220:Disulfides; D046911:Macromolecular Substances; D008565:Membrane Proteins