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Biochem Biophys Res Commun ; 163(1): 161-4, 1989 Aug 30.
Article in English | MEDLINE | ID: mdl-2775257

ABSTRACT

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.


Subject(s)
Diphtheria Toxin/administration & dosage , Luteinizing Hormone/analogs & derivatives , Animals , Cell Line , Cell Survival/drug effects , Diphtheria Toxin/analogs & derivatives , Diphtheria Toxin/toxicity , In Vitro Techniques , Lethal Dose 50 , Mice , Structure-Activity Relationship
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