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The Ammonium Sulfate Inhibition of Human Angiogenin

The Ammonium Sulfate Inhibition of Human Angiogenin

Demetra S M Chatzileontiadou, Vicky G Tsirkone, Kyriaki Dossi, Aikaterini G Kassouni, Panagiota G V Liggri, Anastassia L Kantsadi, George A Stravodimos, Nikolaos A A Balatsos, Vassiliki T Skamnaki, Demetres D Leonidas

FEBS Lett. 2016 Sep;590(17):3005-18.

PMID: 27483019

Abstract:

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR4248743	Angiogenin human			Price

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