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细菌铁载体气杆菌素和肠螯合素从人转铁蛋白中去除铁的结构域偏好性。

Domain preference in iron removal from human transferrin by the bacterial siderophores aerobactin and enterochelin.

作者信息

Ford S, Cooper R A, Evans R W, Hider R C, Williams P H

机构信息

Department of Biochemistry, University of Leicester, England.

出版信息

Eur J Biochem. 1988 Dec 15;178(2):477-81. doi: 10.1111/j.1432-1033.1988.tb14473.x.

Abstract

The ability of the siderophores aerobactin and enterochelin to remove iron from transferrin is reported. Aerobactin removes iron from both high-affinity sites on the transferrin molecule, but shows a marked preference for the C-terminal site. This preference is different to that of many iron chelators. Enterochelin removes iron perferentially from the N-terminal site. No evidence for synergism between aerobactin and bidentate ligands could be detected.

摘要

据报道,铁载体气杆菌素和肠杆菌螯合素具有从转铁蛋白中去除铁的能力。气杆菌素能从转铁蛋白分子上的两个高亲和力位点去除铁,但对C端位点表现出明显的偏好。这种偏好与许多铁螯合剂不同。肠杆菌螯合素优先从N端位点去除铁。未检测到气杆菌素与双齿配体之间存在协同作用的证据。

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