Protein subunit structure in the nuclear envelope has not been previously described. Covalent crosslinking of polypeptides provides a method for studying the subunit structure of protein-rich systems. In this study, several polypeptide crosslinking methods have been used to determine associations among polypeptides in isolated chicken erythrocyte nuclear envelope. Interchain associations that exist in the isolated membrane were fixed by crosslinking the polypeptides in the isolated nuclear envelope. Crosslinked and uncrosslinked polypeptides were resolved by electrophoresis in a dissociating detergent system. Each agent caused distinctive alterations in the gel pattern. Certain bands diminished and disappeared while new bands of two or more times their molecular weight appeared in a reciprocal fashion. Most noteworthy was the major peak of approximately 77,000 daltons molecular weight. This peak crosslinked into dimeric species of approximately 160,000 daltons and higher polymeric species. Some components were distinctly unreactive. The preferential crosslinking reactions indicate that the 77,000 dalton species occur in a specific oligomeric arrangement in the native membrane structure.
| Identifer | oai:union.ndltd.org:vcu.edu/oai:scholarscompass.vcu.edu:etd-5563 |
| Date | 01 January 1977 |
| Creators | Cochran, David Lee |
| Publisher | VCU Scholars Compass |
| Source Sets | Virginia Commonwealth University |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | Theses and Dissertations |
| Rights | © The Author |
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