A superactive hormonotoxin prepared with truncated diphtheria toxin

A chemically truncated form of diphtheria toxin, DT51, which lacks the cell-binding site but retains the membrane-translocating function, was covalently linked to luteinizing hormone (LH) and compared to similar conjugates containing diphtheria toxin (DT) or diphtheria toxin A-chain (DTA). The DT51...

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Veröffentlicht in:	Biochemical and biophysical research communications 1989-08, Vol.163 (1), p.161-164
Hauptverfasser:	Myers, D.A., Villemez, C.L.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cell Line Cell Survival - drug effects Diphtheria Toxin - administration & dosage Diphtheria Toxin - analogs & derivatives Diphtheria Toxin - toxicity Fundamental and applied biological sciences. Psychology In Vitro Techniques Lethal Dose 50 luteinizing hormone Luteinizing Hormone - analogs & derivatives Mice Protein hormones. Growth factors. Cytokines Proteins Structure-Activity Relationship toxins
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Beschreibung
Zusammenfassung:	A chemically truncated form of diphtheria toxin, DT51, which lacks the cell-binding site but retains the membrane-translocating function, was covalently linked to luteinizing hormone (LH) and compared to similar conjugates containing diphtheria toxin (DT) or diphtheria toxin A-chain (DTA). The DT51 hormonotoxin killed cells possessing an LH receptor at concentrations similar to that of DT hormonotoxin and orders of magnitude lower than DTA hormonotoxin. The DTA hormonotoxin exhibited an LD-50 similar to that of previously reported hormonotoxins which employed DTA, ricin A-chain, or gelonin as toxic moieties.
ISSN:	0006-291X 1090-2104
DOI:	10.1016/0006-291X(89)92114-1