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 language | English (US) |
|---|---|
| Pages (from-to) | 1212-1216 |
| Number of pages | 5 |
| Journal | Biochemistry |
| Volume | 17 |
| Issue number | 7 |
| State | Published - 1978 |
| Externally published | Yes |
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- Biochemistry
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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 journal › Article
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TY - JOUR
T1 - In vitro oxidation of intrinsic sulfhydryl groups yields polymers of the two predominant polypeptides in the nuclear envelope fraction
AU - Shelton, Keith Ray
AU - Cochran, David L
PY - 1978
Y1 - 1978
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0017808277&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0017808277&partnerID=8YFLogxK
M3 - Article
C2 - 656384
AN - SCOPUS:0017808277
VL - 17
SP - 1212
EP - 1216
JO - Biochemistry
JF - Biochemistry
SN - 0006-2960
IS - 7
ER -