Interaction of homo-aza-steroidal ester of [p-[bis-(2-chloroethyl) amino]phenyl]acetic acid (ASE) with DNA of Ehrlich ascites tumor cells.
A cytostatic, homo-aza-steroidal ester of [p-[bis-(2-chloroethyl) amino]phenyl]acetic acid (ASE) was reduced with NaB3H4 and [3H]ASE-treated DNA prepared in vitro. We found that: (1) ASE reacts preferentially with purines; (2) ASE decreases the thermal stability of the double helix upon binding to DNA; (3) [3H]ASE binding sites are clustered along the DNA molecules; (4) ASE binding sites probably represent oligo- or polypurine sequences.
D000818:Animals; D000970:Antineoplastic Agents; D001378:Azasteroids; D001894:Borohydrides; D002286:Carcinoma, Ehrlich Tumor / Q000378:metabolism*; D004247:DNA / Q000378:metabolism*; D004355:Drug Stability; D006358:Hot Temperature; D007700:Kinetics; D051379:Mice; D009588:Nitrogen Mustard Compounds / Q000378:metabolism* / Q000494:pharmacology; D009690:Nucleic Acid Conformation / Q000187:drug effects; D010084:Oxidation-Reduction; D011687:Purines / Q000378:metabolism
D000970:Antineoplastic Agents; D001378:Azasteroids; D001894:Borohydrides; D009588:Nitrogen Mustard Compounds; D011687:Purines; C008826:phenacid; C017888:NSC 290205; C025364:sodium borohydride; D004247:DNA