Abstract
Isolated brush border membrane vesicles were prepared from rat kidney cortex for examining the primary interaction between the nephrotoxic aminoglyscoside, gentamicin, and the kidney cell. The uptake of [ 3H]gentamicin was studied kinetically and was found to involve a single class of binding sites (k d = 40.8 μ m and n max = 3.9 nmol/mg protein). Structure-activity relationships were examined by determining the effects of chemically related substances on the uptake. Polyamino acids showed the greatest inhibitory activity, while sugars, polyamines and mono-amino acids were relatively inactive. Inhibition of gentamicin binding was found to be a function of polymer size, but charge did not appear to constitute an important structure-activity requirement for binding to the renal receptor.
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