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肺炎支原体对人乳铁蛋白的获取。

The acquisition of human lactoferrin by Mycoplasma pneumoniae.

作者信息

Tryon V V, Baseman J B

机构信息

Department of Microbiology, University of Texas Health Science Center, San Antonio 78284-7758.

出版信息

Microb Pathog. 1987 Dec;3(6):437-43. doi: 10.1016/0882-4010(87)90013-1.

Abstract

We tested the in vitro binding of human iron-sequestering lactoferrin and transferrin by the mucosal-surface pathogens, Mycoplasma pneumoniae and Mycoplasma genitalium. Mycoplasma pneumoniae bound lactoferrin, but not transferrin, in a saturable and specific manner. Analysis of binding data indicates less than 10,000 lactoferrin receptors per micro-organism with a moderately high binding affinity of 20 nM. No significant binding of lactoferrin or transferrin by M. genitalium was observed.

摘要

我们测试了黏膜表面病原体肺炎支原体和生殖支原体对人铁螯合乳铁蛋白和转铁蛋白的体外结合情况。肺炎支原体以可饱和且特异的方式结合乳铁蛋白,但不结合转铁蛋白。结合数据的分析表明,每个微生物的乳铁蛋白受体少于10000个,结合亲和力适中,为20 nM。未观察到生殖支原体对乳铁蛋白或转铁蛋白有明显结合。

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