Abstract
Nuclease digestion of triton isolated HeLa cell nuclei has resulted in nuclear envelopes containing less than 10% of the nuclear macromolecule. Alkylation and carbamoylation of the nuclear envelope (NE) fraction by chloroethylnitrosoureas (HNU) was disproportionately high (approximately 35% of total nuclear alkylation and approximately 55% carbamoylation) suggesting that the nucleophilic species in the envelope were preferential targets for drug binding. Digestion of the envelope fraction with phospholipase C (PLC), followed by buoyant density gradient separation in Percoll (70%):0.15 M NaCl (30%), demonstrated that some envelope:nucleic acid attachments were destabilized as a result of phospholipid cleavage. In addition, the buoyant density of HNU-modified NE macromolecules was slightly altered by PLC digestion, suggesting that cleavage of polar phospholipids did not completely destabilize the chloroethylated products from the nuclear envelope.
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