Allen G, Gurnett L P
Biochem J. 1983 Feb 1;209(2):481-7. doi: 10.1042/bj2090481.
The locations of the six disulphide bonds and the single free cysteine residue in a variant surface glycoprotein, VSG 117, from the African trypanosome Trypanosoma brucei have been determined to be Cys-14--Cys-140, Cys-121--Cys-182, Cys-389--Cys-404, Cys-398--417, Cys-447--Cys-461 and Cys-455--Cys-468. Cys-244 bears the single thiol group, which is unreactive towards 2-nitro-5-thiocyanobenzoate in the native molecule and is probably buried. Biosynthetically incorporated [35S]cysteine aided the location of the disulphide bonds. Two proteinase-resistant glycosylated domains, each containing two disulphide bonds, were identified in the C-terminal region of the glycoprotein. Details of purification of [35S]cysteine-containing peptides, and Tables of amino acid analyses, are presented in Supplementary Publication SUP 50119 (32 pages), which has been deposited with the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1981) 193,5.
来自非洲锥虫布氏锥虫的一种变异表面糖蛋白VSG 117中六个二硫键和单个游离半胱氨酸残基的位置已确定为：半胱氨酸-14与半胱氨酸-140、半胱氨酸-121与半胱氨酸-182、半胱氨酸-389与半胱氨酸-404、半胱氨酸-398与417、半胱氨酸-447与半胱氨酸-461以及半胱氨酸-455与半胱氨酸-468。半胱氨酸-244带有单个巯基，在天然分子中对2-硝基-5-硫氰基苯甲酸无反应，可能被掩埋。生物合成掺入的[35S]半胱氨酸有助于确定二硫键的位置。在糖蛋白的C端区域鉴定出两个抗蛋白酶的糖基化结构域，每个结构域含有两个二硫键。含[35S]半胱氨酸肽段的纯化细节以及氨基酸分析表见补充出版物SUP 50119（32页），该出版物已存放在英国西约克郡韦瑟比波士顿温泉市大英图书馆出借部，邮编LS23 7BQ，可按《生物化学杂志》（1981年）193,5中所示条件从该处获取复印件。
