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- W2494038384 abstract "In this study, we investigate the inhibition of human angiogenin by ammonium sulfate. The inhibitory potency of ammonium sulfate for human angiogenin ( IC 50 = 123.5 ± 14.9 m m ) is comparable to that previously reported for RN ase A (119.0 ± 6.5 m m ) and RN ase 2 (95.7 ± 9.3 m m ). However, analysis of two X‐ray crystal structures of human angiogenin in complex with sulfate anions (in acidic and basic pH environments, respectively) indicates an entirely distinct mechanism of inhibition. While ammonium sulfate inhibits the ribonucleolytic activity of RN ase A and RN ase 2 by binding to the active site of these enzymes, sulfate anions bind only to peripheral substrate anion‐binding subsites of human angiogenin, and not to the active site." @default.
- W2494038384 created "2016-08-23" @default.
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- W2494038384 date "2016-08-12" @default.
- W2494038384 modified "2023-10-05" @default.
- W2494038384 title "The ammonium sulfate inhibition of human angiogenin" @default.
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- W2494038384 doi "https://doi.org/10.1002/1873-3468.12335" @default.
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