The effect of the lysosomotropic drug chloroquine on the binding of N-acetyl-beta-D-glucosaminidase to mannose-6-phosphate recognizing receptors of rat liver.
The binding of N-acetyl-beta-D-glucosaminidase to rat liver receptors was studied in the presence of chloroquine. The association rate constant was not affected in the presence of the drug, while the dissociation rate constant and consequently the equilibrium dissociation binding constant significatively decreased. This results may explain effects of chloroquine on lysosomal enzyme transport found in cultured cells by other authors.
Sosa
M A
MA
Bertini
F
F
D000118:Acetylglucosaminidase / Q000378:metabolism*; D000818:Animals; D001692:Biological Transport; D002352:Carrier Proteins / Q000378:metabolism*; D002738:Chloroquine / Q000494:pharmacology*; D006596:Hexosaminidases / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D051381:Rats; D017527:Receptor, IGF Type 2
D002352:Carrier Proteins; D017527:Receptor, IGF Type 2; D002738:Chloroquine; D006596:Hexosaminidases; D000118:Acetylglucosaminidase