The major metabolite of bendazac inhibits the glycosylation of soluble lens proteins: a possible mechanism for a delay in cataractogenesis.
Glucose-6-phosphate and galactose react non-enzymically with lens proteins. The rates of these reactions are decreased by 5-hydroxybendazac but not by its parent compound, bendazac. Both bendazac and its major metabolite bind to lens proteins, mostly by non-covalent interactions. These results are discussed in relation to the use of bendazac as an anti-cataract drug.
Lewis
B S
BS
Nuffield Laboratory of Ophthalmology, University of Oxford.
Harding
J J
JJ
D000818:Animals; D002386:Cataract / Q000517:prevention & control*; D002417:Cattle; D003459:Crystallins / Q000378:metabolism*; D005690:Galactose / Q000378:metabolism; D005958:Glucosephosphates / Q000378:metabolism; D006031:Glycosylation; D066298:In Vitro Techniques; D007191:Indazoles / Q000494:pharmacology* / Q000627:therapeutic use; D011485:Protein Binding; D011720:Pyrazoles / Q000494:pharmacology*
D003459:Crystallins; D005958:Glucosephosphates; D007191:Indazoles; D011720:Pyrazoles; C051605:5-hydroxybendazac; C000123:bendazac; D005690:Galactose