Schell D, Evers R, Preis D, Ziegelbauer K, Kiefer H, Lottspeich F, Cornelissen A W, Overath P
Max-Planck-Institut für Biologie, Tübingen, FRG.
EMBO J. 1991 May;10(5):1061-6. doi: 10.1002/j.1460-2075.1991.tb08045.x.
A transferrin-binding protein (TFBP) with an apparent molecular weight of 42 kd was purified from detergent-soluble membrane proteins of bloodstream forms of Trypanosoma brucei. The protein is not expressed in the insect-borne stage of the parasite's life-cycle. Purified TFBP can be converted from an amphiphilic to a hydrophilic form by cleavage with T.brucei glycosylphosphatidylinositol (GPI)-specific phospholipase C, demonstrating that the C-terminus is modified by a GPI-membrane anchor. The TFBP is encoded by an expression-site-associated gene [ESAG 6 in the nomenclature of Pays et al. (1989) Cell, 57, 835-845] which is under the control of the promoter transcribing the expressed variant surface glycoprotein gene. The possible function of TFBP as a receptor for the uptake of transferrin in bloodstream forms is discussed.
从布氏锥虫血流形式的去污剂可溶性膜蛋白中纯化出一种表观分子量为42kd的转铁蛋白结合蛋白（TFBP）。该蛋白在寄生虫生命周期的昆虫传播阶段不表达。纯化的TFBP可通过用布氏锥虫糖基磷脂酰肌醇（GPI）特异性磷脂酶C切割，从两亲形式转变为亲水形式，表明其C末端被GPI膜锚修饰。TFBP由一个表达位点相关基因编码[在Pays等人（1989年）《细胞》，57卷，835 - 845页的命名法中为ESAG 6]，该基因受转录表达的可变表面糖蛋白基因的启动子控制。讨论了TFBP作为血流形式中转铁蛋白摄取受体的可能功能。
