TY - JOUR
T1 - The ammonium sulfate inhibition of human angiogenin
AU - Chatzileontiadou, Demetra S.M.
AU - Tsirkone, Vicky G.
AU - Dossi, Kyriaki
AU - Kassouni, Aikaterini G.
AU - Liggri, Panagiota G.V.
AU - Kantsadi, Anastassia L.
AU - Stravodimos, George A.
AU - Balatsos, Nikolaos A.A.
AU - Skamnaki, Vassiliki T.
AU - Leonidas, Demetres D.
PY - 2016/9/1
Y1 - 2016/9/1
N2 - 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.
AB - 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.
KW - ammonium sulfate
KW - angiogenin
KW - expression and purification
KW - molecular cloning
KW - neovascularization
KW - X-ray crystallography
UR - http://www.scopus.com/inward/record.url?scp=84985906119&partnerID=8YFLogxK
U2 - 10.1002/1873-3468.12335
DO - 10.1002/1873-3468.12335
M3 - Letter
C2 - 27483019
AN - SCOPUS:84985906119
SN - 0014-5793
VL - 590
SP - 3005
EP - 3018
JO - FEBS Letters
JF - FEBS Letters
IS - 17
ER -