Secretion of an inhibitor of follicle-stimulating hormone binding to receptor by the bacteria Serratia, including a strain isolated from porcine follicular fluid.

Secretion of an inhibitor of follicle-stimulating hormone binding to receptor by the bacteria Serratia, including a strain isolated from porcine follicular fluid.
复制标题

沙雷氏菌(包括从猪卵泡液中分离出的菌株)分泌与受体结合的促卵泡激素抑制剂。

DOI:
--
复制
发表时间:
1984
影响因子:
3.6
通讯作者:
L. Reichert
L. Reichert
中科院分区:
生物学2区
文献类型:
--
作者:
P. Sluss;L. Reichert

文献摘要

参考文献

被引文献

相似文献

细菌在受污染的猪卵泡液(PFF)中的生长与结合到小牛睾丸膜上的125I-FSH的大分子(Mr大于6000)抑制剂(FSH-BI)浓度增加有关(Sluss和Reichert,1983)。我们承诺对细菌进行鉴定,并确定该抑制剂是否是分泌型产品。从PFF中分离的39个纯细菌菌落中只有1个产生FSH-BI。该细菌被初步鉴定为液化沙雷氏菌,随后被证明在合成培养基中也能分泌FSH-BI。来自PFF的液化沙雷氏菌在仅以葡萄糖为碳源的最低限度培养基中分泌FSH-BI。其他细菌,包括假单胞菌和链球菌,在无菌PFF或合成培养基中都不分泌FSH-BI。从美国典型培养物库获得的6株沙雷氏菌也能分泌FSH-BI。液化沙雷氏菌分泌的FSH-BI经加热(60℃时T1/2=30min)、pH 2(25℃下2 h)灭活,不溶于乙醚、75%丙酮或40%硫酸铵。在有效抑制~(125)I-FSH结合的FSH-BI剂量(50%)中,未检测到使用酪蛋白底物的蛋白酶活性。初步研究表明,FSH-BI是由于对膜的影响,而不是对放射性配基的影响。这些数据表明,从PFF分离的液化沙雷氏菌分泌一种MR大于6000的物质,该物质能抑制125I-hFSH的受体结合。此外,FSH-BI似乎是由所测试的所有(7)沙雷氏菌菌株组成地分泌的。
Bacterial growth in contaminated porcine follicular fluid (PFF) was associated with increased concentrations of a large molecular weight (Mr greater than 6000) inhibitor (FSH-BI) of 125I-FSH binding to calf testis membranes (Sluss and Reichert, 1983). We undertook to identify the bacteria and to determine if the inhibitor was a secretory product. Only one of 39 pure bacterial colonies isolated from PFF generated FSH-BI. The bacterium was tentatively identified as Serratia liquifaciens and was subsequently shown to also secrete FSH-BI when grown in synthetic culture media. Serratia liquifaciens from PFF secreted FSH-BI in a minimal culture medium containing only glucose as a carbon source. Other bacteria, including strains of Pseudomonas and Streptococcus did not secrete FSH-BI in either sterile PFF or synthetic culture media. Six strains of Serratia, obtained from the American Type Culture Collection, also secreted FSH-BI. FSH-BI secreted by Serratia liquifaciens was inactivated by heat (T 1/2 = 30 min at 60 degrees C), exposure to pH 2 (2 h at 25 degrees C) and was insoluble in ether, 75% acetone or 40% ammonium sulfate. Protease activity, using a casein substrate, was undetected in doses of FSH-BI which effectively (50%) inhibited 125I-FSH binding. Initial studies suggested that FSH-BI was due to effects on membranes rather than on the radioligand. These data demonstrate that Serratia liquifaciens isolated from PFF secretes a substance of Mr greater than 6000 which inhibits receptor binding of 125I-hFSH. Furthermore, the FSH-BI appears to be secreted constitutively by all (7) strains of Serratia tested.
DOI: --
发表时间: 1982
期刊: The Journal of biological chemistry
影响因子: --
作者:
Andersen,TT;ReichertJr,LE
通讯作者: ReichertJr,LE