Competitive binding of adenine and nicotinamide–adenine dinucleotide to diphtheria toxin
نویسندگان
چکیده
منابع مشابه
Interaction of fragment A from diphtheria toxin with nicotinamide adenine dinucleotide.
This reaction is catalyzed by Fragment A (mol wt 24,000) or other less common fragments generated by limited proteolysis and reduction of the toxin, but not by the toxin itself (mol wt 63,000). This report describes studies of the interaction of NAD+ with Fragment A. In addition to its major enzymic activity, Fragment A also catalyzes the slow hydrolysis of the nicotinamide-ribose linkage of NAD+.
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Two substances possessing the ability to bind to diphtheria toxin (DT) were found to be present in a membrane fraction from DT-sensitive Vero cells. One of these substances was found on the basis of its ability to bind DT and inhibit its cytotoxic effect. This inhibitory substance competitively inhibited the binding of DT to Vero cells. However this inhibitor could not bind to CRM197, the produ...
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The biochemical characteristics of specific receptor molecules for diphtheria toxin on the surface of two toxin-sensitive cell lines (Vero and BS-C-1) were examined. Diphtheria toxin was found to bind to a number of different proteins in Nonidet P-40 solubilized extracts of 125I-labeled cells. In contrast, permitting diphtheria toxin to bind first to labeled intact cells, which were subsequentl...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1968
ISSN: 0306-3283
DOI: 10.1042/bj1070730