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牛乳铁蛋白与无乳链球菌的结合

Binding of bovine lactoferrin to Streptococcus agalactiae.

作者信息

Rainard P

机构信息

Institut National de la Recherche Agronomique, Laboratoire de Pathologie Infectieuse et Immunologie, Nouzilly, France.

出版信息

FEMS Microbiol Lett. 1992 Nov 1;77(1-3):235-9. doi: 10.1016/0378-1097(92)90162-h.

Abstract

Bovine lactoferrin is an iron-binding protein present in mammary gland secretions. The exposure of Streptococcus agalactiae to bovine lactoferrin resulted in the binding of this protein to all the 12 strains of bovine origin tested, and also, although to a lesser degree, to the five tested strains of human origin. The interaction of lactoferrin with one high-binding bovine strain (24/60, the prototype NT/X strain) was studied. Binding was time-dependent, dose-dependent, and saturable. The binding of lactoferrin was slightly affected by cultivation conditions, and appeared to be heat-stable. The binding of biotinylated lactoferrin was inhibited by unlabelled lactoferrin but not by bovine serum albumin.

摘要

牛乳铁蛋白是一种存在于乳腺分泌物中的铁结合蛋白。无乳链球菌暴露于牛乳铁蛋白后,该蛋白与所有测试的12株牛源菌株结合,对于5株测试的人源菌株也有结合,不过程度较轻。研究了乳铁蛋白与一株高结合性牛源菌株(24/60,NT/X原型菌株)的相互作用。结合具有时间依赖性、剂量依赖性且可饱和。乳铁蛋白的结合受培养条件的影响较小,且似乎具有热稳定性。生物素化乳铁蛋白的结合受到未标记乳铁蛋白的抑制,但不受牛血清白蛋白的抑制。

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