Aluminum interrupts the formation of alkaline-ribonuclease-inhibitor complex from bovine brain.
The effect of aluminum on alkaline ribonuclease (RNase) and RNase inhibitor, purified from bovine brain, was investigated. Incubation of alkaline RNase with aluminum interrupted binding of RNase inhibitor to alkaline RNase. A stoichiometry of 1:1 for the binding of aluminum to brain alkaline RNase was estimated, whereas no aluminum was found to be bound to the RNase inhibitor. Aluminum-bound alkaline RNase, however, retained a full alkaline RNase activity. None of the enzyme-bound aluminum was dissociated by dialysis against 50 mM Hepes, pH 7.0, at 4 degrees C for 24 h. Citrate, EDTA, NaF and apotransferrin protected the alkaline RNase against aluminum binding. Aluminum did not bind to the incubated alkaline RNase-inhibitor complex, suggesting that aluminum might compete with RNase inhibitor for the binding site. However, the data from chemical modification and spectroscopic studies indicate that it is also highly possible that aluminum binding to the enzyme induces conformational changes at or near the inhibitor-binding site, which subsequently interrupt binding of RNase inhibitor to alkaline RNase. These results suggest that accumulation of aluminum in brain might affect the regulation of RNA metabolism.
Department of Biochemistry, College of Medicine, University of Ulsan, Seoul, Korea.
S W
SW
Cho
G Y
GY
Kim
D000535:Aluminum / Q000378:metabolism / Q000494:pharmacology*; D000818:Animals; D001665:Binding Sites; D001921:Brain / Q000201:enzymology*; D002417:Cattle; D002614:Chelating Agents; D002850:Chromatography, Gel; D006639:Histidine / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D008239:Lysine / Q000737:chemistry; D011487:Protein Conformation; D012260:Ribonucleases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D013053:Spectrophotometry
D002614:Chelating Agents; D006639:Histidine; D000535:Aluminum; D012260:Ribonucleases; D008239:Lysine