Effects of Aminoglycoside Antibiotics on Lysosomal Enzymes of Rat Kidney

概要

論文の詳細を見る
The binding of three aminoglycoside antibiotics, gentamicin, amikacin, and 3', 4'-dideoxykanamycin B, to various lysosomal enzymes, N-acetyl-β-D-glucosaminidase, acid phosphatase, and lysozyme, was examined in vitro by using an affinity column of 3', 4'-dideoxykanamycin B-conjugated Sepharose 4B in order to investigate the mechanism of the accumulation of aminoglycoside antibiotics in the kidney. N-Acetyl-β-D-glucosaminidase and lysozyme were bound to the affinity column, but acid phosphatase was not adsorbed on the column. The activity of lysozyme was strongly inhibited by the addition of the three aminoglycosides at the concentration of 1 mM. In the case of N-acetyl-β-D-glucosaminidase, the activity was significantly inhibited in the presence of amikacin, but, in contrast, the activity was slightly activated by the addition of gentamicin or 3', 4'-dideoxykanamycin B. Acid phosphatase activity was not affected by the addition of any of the aminoglycosides. Lineweaver-Burk plots indicate that the inhibition of N-acetyl-β-D-glucosaminidase by amikacin is competitive. In the case of lysozyme, competitive inhibition by all three aminoglycosides was observed with Micrococcus luteus cells as the substrate. These findings indicate that the lysosomal enzyme activities may be influenced by the binding of aminoglycosides, and this binding may represent one of the accumulation mechanisms of aminoglycosides in the kidney.
社団法人日本薬学会の論文
1983-09-25

Effects of Aminoglycoside Antibiotics on Lysosomal Enzymes of Rat Kidney

スポンサーリンク

概要

著者

関連論文

スポンサーリンク