Structures of glycophosphosphingolipids of Tritrichomonas foetus: a novel glycophosphosphingolipid.
Structures of glycophosphosphingolipids of Tritrichomonas foetus: a novel glycophosphosphingolipid.
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DOI：
10.1016/0003-9861(91)90059-r
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发表时间：
1991-05
影响因子：
3.9
通讯作者：
B. Singh;C. Costello;D. Beach
中科院分区：
文献类型：
--
作者：
B. Singh;C. Costello;D. Beach
胎儿三毛单胞菌（一种牛泌尿生殖道的耐氧寄生虫）的糖磷鞘脂已通过代谢标记、色谱和串联质谱的组合进行了表征。T.经DEAE-SephadexA-25柱层析分离得到的胎儿脂肪经高效薄层层析进一步分离，并经高效液相层析纯化得到其组分脂质。两个非皂化脂质组分，指定TF 1和TF 2，可以代谢标记与[3 H]肌醇和[32 P]正磷酸。[3 H]岩藻糖和[14 C]乙醇胺优先掺入TF 1馏分中。TF 1被α-岩藻糖苷酶部分水解。TF 1和TF 2都含有神经酰胺，其中含量最丰富的神经酰胺含有二氢鞘氨醇或鞘氨醇以及16：0 N-酰基。TF 2含有肌醇磷酸神经酰胺。另一方面，TF 1含有三种密切相关的组分，其中岩藻糖与肌醇二磷酸连接，其中一种磷酸与神经酰胺部分连接，另一种磷酸游离或与乙醇胺或N-乙酰乙醇胺连接。TF 1是一种新型的糖磷鞘脂，与真核细胞膜蛋白的糖基磷脂酰肌醇锚具有一定的结构相似性。
The glycophosphosphingolipids ofTritrichomonas foetus, an aerotolerant parasite of the urogenital tract of cattle, have been characterized by a combination of metabolic labeling, chromatography, and tandem mass spectrometry. The acidic glycolipid fraction ofT. foetusobtained by DEAE Sephadex A-25 column chromatography was subfractionated by high performance thin layer chromatography and the component lipids were purified by high performance liquid chromatography. Two nonsaponifiable lipid fractions, designated TF1and TF2, could be metabolically labeled with [3H]myoinositol and [32P]orthophosphate. [3H]Fucose and [14C]ethanolamine were preferentially incorporated into the TF1fraction. TF1was partially hydrolyzed by α-fucosidase. Both TF1and TF2contain ceramides, the most abundant having either sphinganine or sphingosine and a 16:0N-acyl group. TF2contains inositolphosphoceramides. TF1, on the other hand, contains three closely related components, in each of which fucose is linked to inositol diphosphate with one of the phosphates linked to the ceramide moiety and the other phosphate either free or linked to ethanolamine orN-acetylethanolamine. TF1appears to be a novel class of glycophosphosphingolipid which shows some structural similarities to the glycosylphosphatidylinositol anchors of eukaryotic membrane proteins.