In vitro oxidation of intrinsic sulfhydryl groups yields polymers of the two predominant polypeptides in the nuclear envelope fraction

Keith Ray Shelton, David L Cochran

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

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 o-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 our 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.

Original languageEnglish (US)
Pages (from-to)1212-1216
Number of pages5
JournalBiochemistry
Volume17
Issue number7
StatePublished - 1978
Externally publishedYes

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Nuclear Envelope
Polymers
Oxidation
Peptides
Nuclear Proteins
Oligomers
Skeleton
Dimers
Solubility
Erythrocytes
In Vitro Techniques
Ions
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

In vitro oxidation of intrinsic sulfhydryl groups yields polymers of the two predominant polypeptides in the nuclear envelope fraction. / Shelton, Keith Ray; Cochran, David L.

In: Biochemistry, Vol. 17, No. 7, 1978, p. 1212-1216.

Research output: Contribution to journalArticle

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