Abstract
The affinity of proteins for nitrocellulose filters has been exploited in quantitating protein-ligand interactions. The applicability of this method to studying the interaction between the purified first enzyme of l-histidine biosynthesis of Salmonella typhimurium, ATP phosphoribosyltransferase, and histidyl-tRNA is examined. A systematic study of the effects of environmental factors on formation of the complex and on retention of the complex by the filter is reported.
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