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 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.
Department of Molecular Biology, University of Wyoming, Laramie 82071-3944.
D A
DA
Myers
C L
CL
Villemez
D000818:Animals; D002460:Cell Line; D002470:Cell Survival / Q000187:drug effects; D004167:Diphtheria Toxin / Q000008:administration & dosage* / Q000031:analogs & derivatives / Q000633:toxicity; D066298:In Vitro Techniques; D007928:Lethal Dose 50; D007986:Luteinizing Hormone / Q000031:analogs & derivatives*; D051379:Mice; D013329:Structure-Activity Relationship
D004167:Diphtheria Toxin; D007986:Luteinizing Hormone