Binding of 3',4'-dideoxykanamycin B to ATP and its related compounds.
The interactions of aminoglycoside, 3',4'-dideoxykanamycin B(DKB) with ATP and its related compounds were investigated. ATP, ADP, cyclic AMP and FAD bound to the DKB-conjugated Sepharose 4B column. The binding of DKB to ATP was also confirmed by equilibrium gel filtration. In the acidic pH region, the fluorescence of nucleotides was quenched by DKB. The Stern-Volmer plots showed that the molar ratios of the complexes were 1:1. The apparent stability constant was dependent on the number of the phosphate groups of nucleotides and was in the order of ATP greater than ADP greater than AMP.
D000241:Adenosine / Q000378:metabolism; D000244:Adenosine Diphosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism*; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D000242:Cyclic AMP / Q000378:metabolism; D003982:Dibekacin / Q000009:adverse effects / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D007612:Kanamycin / Q000031:analogs & derivatives*; D007674:Kidney Diseases / Q000139:chemically induced; D007687:Kidney Tubules, Proximal / Q000378:metabolism; D013050:Spectrometry, Fluorescence
D003982:Dibekacin; D007612:Kanamycin; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D000242:Cyclic AMP; D000241:Adenosine