Antitumor lectin-trypsin inhibitor conjugate.
Concanavalin A (Con A) and trypsin inhibitor isolated from Acacia confusa were covalently linked with N-succinimidyl-3-(2-pyridyldithio)propionate. Con A-A. confusa trypsin inhibitor (ACTI) conjugate covalently bound (Con A-ACTI) retained about 42% of the trypsin inhibitory activity present in the native ACTI and had a higher hemagglutinating activity than did the native Con A. Con A-ACTI had a greater resistance to tryptic digestion than did the mixture of Con A and ACTI. The conjugate entered sarcoma 180 tumor cells, whereas the free ACTI did not. A single dose of the conjugate injected ip into noninbred N:NIH(S) white mice bearing sarcoma 180 had a remarkable effect of increasing the survival of tumor-bearing mice, while the mixture of an equivalent dose of free Con A and ACTI was not effective.
D000818:Animals; D002455:Cell Division / Q000187:drug effects; D002460:Cell Line; D002463:Cell Membrane Permeability / Q000187:drug effects; D002850:Chromatography, Gel; D003208:Concanavalin A / Q000138:chemical synthesis / Q000378:metabolism / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D006386:Hemagglutination Tests; D051379:Mice; D010447:Peptide Hydrolases / Q000378:metabolism; D011485:Protein Binding; D012510:Sarcoma 180 / Q000378:metabolism* / Q000473:pathology; D014361:Trypsin Inhibitors / Q000138:chemical synthesis / Q000378:metabolism / Q000494:pharmacology*
D014361:Trypsin Inhibitors; D003208:Concanavalin A; D010447:Peptide Hydrolases