DOI
https://doi.org/10.25772/6YJR-YK46
Defense Date
1977
Document Type
Thesis
Degree Name
Master of Science
Department
Biochemistry
First Advisor
Keith R. Shelton
Abstract
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.
Rights
© The Author
Is Part Of
VCU University Archives
Is Part Of
VCU Theses and Dissertations
Date of Submission
8-30-2016