| Literature DB >> 1845367 |
D Schell1, R Evers, D Preis, K Ziegelbauer, H Kiefer, F Lottspeich, A W Cornelissen, P Overath.
Abstract
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.Entities:
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Year: 1991 PMID: 1845367 PMCID: PMC452758 DOI: 10.1002/j.1460-2075.1991.tb08045.x
Source DB: PubMed Journal: EMBO J ISSN: 0261-4189 Impact factor: 11.598