Chimeric toxins: Toxic, disulfide-linked conjugate of concanavalin A with fragment A from diphtheria toxin
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منابع مشابه
Chimeric toxins: toxic, disulfide-linked conjugate of concanavalin A with fragment A from diphtheria toxin.
A disulfide-linked conjugate of concanavalin A (Con A) and fragment A from diphtheria toxin has been synthesized and shown to be toxic for HeLa (human), Chinese hamster ovary (CHO), and SV3T3 (murine) cells. The conjugate was constructed by first coupling cystamine to Con A with a carbodiimide reagent and then reacting the modified Con A with reduced fragment A under conditions promoting disulf...
متن کاملCharacterization of a transferrin-diphtheria toxin conjugate.
We report here the synthesis and properties of a hybrid toxin prepared by covalently coupling diphtheria toxin to transferrin. The purified material contained two major hybrid protein species and was highly cytotoxic to mouse LMTK- cells in culture, reducing protein synthesis by 50% in 24 h at a concentration of 1 ng/ml. Cytotoxic activity was completely abolished in the presence of exogenous t...
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The biochemical and biologic properties of a purified disulfide conjugate of diphtheria toxin fragment A and human placental lactogen (toxin A-hPL) have been studied by (a) assaying the ADP-ribosyltransferase activity of the intact conjugate, (b) assaying the binding of the intact conjugate to mammary gland plasma membrane lactogenic receptors, and (c) assaying the effect of the conjugate on th...
متن کاملAmino-acid sequence of fragment A, an enzymically active fragment from diphtheria toxin.
The amino-acid sequence of Fragment A from diphtheria toxin is reported. Fragment A (molecular weight, Mr, 21,145) is the major enzymically active fragment produced upon activation of the intact toxin (Mr about 60,000) by limited tryptic digestion and reduction. It, or a similar fragment, is believed responsible for the inhibition of protein synthesis in animal cells exposed to the toxin. Fragm...
متن کاملInteraction 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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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1978
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.75.11.5319