The ammonium sulfate inhibition of human angiogenin.

Autor: Chatzileontiadou DS; Department of Biochemistry and Biotechnology, University of Thessaly, Larissa, Greece., Tsirkone VG; Institute of Biology, Medicinal Chemistry & Biotechnology, National Hellenic Research Foundation, Athens, Greece., Dossi K; Institute of Biology, Medicinal Chemistry & Biotechnology, National Hellenic Research Foundation, Athens, Greece., Kassouni AG; Department of Biochemistry and Biotechnology, University of Thessaly, Larissa, Greece., Liggri PG; Department of Biochemistry and Biotechnology, University of Thessaly, Larissa, Greece., Kantsadi AL; Department of Biochemistry and Biotechnology, University of Thessaly, Larissa, Greece., Stravodimos GA; Department of Biochemistry and Biotechnology, University of Thessaly, Larissa, Greece., Balatsos NA; Department of Biochemistry and Biotechnology, University of Thessaly, Larissa, Greece., Skamnaki VT; Department of Biochemistry and Biotechnology, University of Thessaly, Larissa, Greece., Leonidas DD; Department of Biochemistry and Biotechnology, University of Thessaly, Larissa, Greece.
Jazyk: angličtina
Zdroj: FEBS letters [FEBS Lett] 2016 Sep; Vol. 590 (17), pp. 3005-18. Date of Electronic Publication: 2016 Aug 12.
DOI: 10.1002/1873-3468.12335
Abstrakt: In this study, we investigate the inhibition of human angiogenin by ammonium sulfate. The inhibitory potency of ammonium sulfate for human angiogenin (IC50 = 123.5 ± 14.9 mm) is comparable to that previously reported for RNase A (119.0 ± 6.5 mm) and RNase 2 (95.7 ± 9.3 mm). 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 RNase A and RNase 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.
(© 2016 Federation of European Biochemical Societies.)
Databáze: MEDLINE
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