Abstract
The basic amino acids arginine and its lower homologue, α-amino-γ-guanidinobutyric acid, increased the intracellular levels of melphalan only in the presence of leucine and sodium ions. This increase occurred solely through the monovalent cation-dependent, high-affinity, leucine-preferring transport system, one of the two amino acid transport systems responsible for melphalan uptake. Acceleration of melphalan exodus by leucine is antagonized by α-amino-γ-guanidinobutyric acid, resulting in increased cellular retention of melphalan.
- Copyright © 1981 by The American Society for Pharmacology and Experimental Therapeutics
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