Interaction of mechlorethamine and isophosphamide with bovine serum albumin and rat liver microsomes

✍ Scribed by Larry M. Allen; Patrick J. Creaven

• Book ID: 102405234
• Publisher: John Wiley and Sons
• Year: 1973
• Tongue: English
• Weight: 307 KB
• Volume: 62
• Category: Article
• ISSN: 0022-3549
• DOI: 10.1002/jps.2600620545

✦ Synopsis

The interaction of the alkylating metabolites of isophosphamidc and mechlorethamine with microsomal protein and bovinc serum albumin was studied. The procedure of freezing and thawing of rat liver microsomal fraction greatly increases the inhibition by mechlorethamine of its ethylmorphine demethylase activity. Microsomal metabolites of isophosphamide bind covalently to microsomal protein and bovine serum albumin. Mechlorethamine interacts with thiol and tyrosyl hydroxyl groups of bovine serum albumin. The use of the mechlorethamine-bovine serum albumin interaction as a model system for the study of the reactions of isophosphamide metabolites with protein is proposed.