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- W4244610050 abstract "Inhibitory study of RNase L with ferric ion was performed to clarify the function of the enzyme. The maximal inhibitory pH of ferric ion for the enzyme is in 3.5 ~ 5.0 and the type of inhibition is found to be competitive with the substrate. The Km for RNA and Ki of ferric ion are 1.54 × 10−1 mg/ml and 22.5 µM, respectively. As the recovery of activity from iron-inactivated RNase L is almost completely realized by dialysis against EDTA solution, the inhibition of RNase L with ferric ion is considered to be a reversible reaction. Moreover, the enzyme is rapidly inactivated by methylene blue- or rose bengal-sensitized photooxidation, but the photoinactivation of RNase L is protected in the presence of the competitive inhibitor, ferric ion. It may reasonably be taken as an evidence that ferric ion attacks the active site of the enzyme." @default.
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- W4244610050 date "1978-06-01" @default.
- W4244610050 modified "2023-09-26" @default.
- W4244610050 title "Inhibitory Study of Ribonuclease L fromAspergillussp. with Ferric Ion" @default.
- W4244610050 doi "https://doi.org/10.1080/00021369.1978.10863137" @default.
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