Ferguson M A, Snary D, Allen A K
Biochim Biophys Acta. 1985 Sep 27;842(1):39-44. doi: 10.1016/0304-4165(85)90290-9.
Cell surface glycoconjugates of epimastigotes of Trypanosoma cruzi have been isolated and analyzed to give their amino acid and carbohydrate compositions. Those which have been investigated are a complex of three closely associated glycoproteins, GP24, GP31, GP37, and a lipopeptidophosphoglycan. The GP24-GP31-GP37 complex has an unusual amino acid composition with very low levels of hydrophobic amino acids, it contains 56% (w/w) carbohydrate, with mannose, galactose and glucosamine (presumably N-acetyl) being present in approximately equal quantities. The lipopeptidophosphoglycan also has low levels of hydrophobic amino acids and contains equal levels of mannose and galactose together with lesser amounts of (N-acetyl) glucosamine. The glycoconjugates are contrasted and compared with two other previously characterised cell surface glycoproteins (GP25 and GP72) from T. cruzi.
克氏锥虫前鞭毛体的细胞表面糖缀合物已被分离并分析,以确定其氨基酸和碳水化合物组成。已研究的糖缀合物包括三种紧密相关的糖蛋白GP24、GP31、GP37的复合物,以及一种脂肽磷聚糖。GP24 - GP31 - GP37复合物具有不寻常的氨基酸组成,疏水氨基酸水平非常低,它含有56%(w/w)的碳水化合物,甘露糖、半乳糖和葡糖胺(可能是N - 乙酰化的)含量大致相等。脂肽磷聚糖的疏水氨基酸水平也较低,含有等量的甘露糖和半乳糖以及较少的(N - 乙酰)葡糖胺。将这些糖缀合物与克氏锥虫另外两种先前已表征的细胞表面糖蛋白(GP25和GP72)进行了对比和比较。