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奎宁特异性抑制肺炎链球菌F0F1 H+ -ATP酶的蛋白脂质亚基。

Quinine specifically inhibits the proteolipid subunit of the F0F1 H+ -ATPase of Streptococcus pneumoniae.

作者信息

Muñoz R, García E, De la Campa A G

机构信息

Centro Nacional de Biología Celular y Retrovirus, Instituto de Salud Carlos III, Majadahonda, Spain.

出版信息

J Bacteriol. 1996 Apr;178(8):2455-8. doi: 10.1128/jb.178.8.2455-2458.1996.

Abstract

Streptococcus pneumoniae is uniquely sensitive to quinine and its derivatives, but only those alkaloids having antimalarial properties, i.e., those in the erythro configuration, also possess antipneumococcal activity. Quinine and related compounds inhibit the pneumococcal H+ -ATPase. Quinine- and optochin-resistant pneumococci showed mutations that change amino acid residues located in one of the two transmembrane alpha-helices of the c subunit of the F0F1, H+ -ATPase.

摘要

肺炎链球菌对奎宁及其衍生物具有独特的敏感性,但只有那些具有抗疟特性的生物碱,即具有赤型构型的生物碱,才具有抗肺炎球菌活性。奎宁及相关化合物可抑制肺炎球菌的H⁺-ATP酶。对奎宁和奥普托欣耐药的肺炎球菌显示出突变,这些突变改变了位于F₀F₁、H⁺-ATP酶c亚基两个跨膜α螺旋之一中的氨基酸残基。

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Quinidine in falciparum malaria.奎宁在恶性疟中的应用。
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