Abstract
In the DPN-DPNase system that catalyzes the (imidazolytic) breakdown of pyridine coenzymes, l-histidine and imidazoleacetic acid were found practically unreactive. The reactivity of the latter compound could be restored by esterification to imidazoleacetic acid ethylester. Imidazole, the parent compound of these heterocycles, and acetylhistamine exhibited normal reactivity. The dinucleotides (imidazolytic products) corresponding to the above compounds were isolated and their properties were studied.
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