Gomes V, Huet-Duvillier G, Aubert J P, Dirat I, Tetaert D, Moncany M L, Richet C, Vervoort T, Pays E, Degand P
Arch Biochem Biophys. 1986 Sep;249(2):427-36. doi: 10.1016/0003-9861(86)90019-6.
A specific surface glycoprotein of a variant of Trypanosoma brucei was cleaved with trypsin and the two major domains of the molecule have been purified. We have studied the chemical composition of each domain and compared the data to published results of the specific cDNA sequence. Circular dichroism measurements show that the amino-terminal domain includes preferentially alpha-helical or beta-sheet structure. The physicochemical analyses are supplemented by a prediction of secondary structure and a statistical pattern of hydrophilicity-hydrophobicity. The results are discussed in light of the internal limits that were described in the process of partial gene conversion occurring between the variant gene sequence and related members of the same gene family. Immunoblots with homologous antiserum indicate that the amino-terminal domain is implicated in antigenicity. In addition, immunoblotting with heterologous antiserum on native antigen, tryptic hydrolysates, or purified domains suggests a site of interaction supported by the two domains.
用胰蛋白酶切割了布氏锥虫一个变体的一种特异性表面糖蛋白，该分子的两个主要结构域已被纯化。我们研究了每个结构域的化学组成，并将数据与已发表的特定cDNA序列结果进行了比较。圆二色性测量表明，氨基末端结构域优先包含α-螺旋或β-折叠结构。通过二级结构预测和亲水-疏水性统计模式对物理化学分析进行了补充。根据在变体基因序列与同一基因家族相关成员之间发生的部分基因转换过程中所描述的内部限制来讨论结果。用同源抗血清进行的免疫印迹表明氨基末端结构域与抗原性有关。此外，用异源抗血清对天然抗原、胰蛋白酶水解产物或纯化结构域进行免疫印迹，提示两个结构域支持一个相互作用位点。
