Talamás-Rohana P, Rosales-Encina J L, Gutiérrez M C, Hernández V I
Departamento de Patología Experimental, Centro de Investigación y de Estudios Avanzados, México DF, México.
Arch Med Res. 1992;23(2):119-23.
A 37 kDa protein has been described as a putative receptor for fibronectin (Fn) on E. histolytica trophozoites (1). We have now identified a membrane protein that binds biotinylated fibronectin (BFn) with an apparent molecular weight of 140 kDa. Using BFn we were able to follow this protein during partial purification through DEAE-cellulose and Fn-Sepharose chromatography. Antisera prepared against a peptide corresponding to the deduced amino acid sequence for the putative receptor binding site for human Fn (2) recognized a protein with the same molecular weight. The purified protein was also recognized by this sera. We propose that this protein may function as a Fn receptor and will explore the possibility for it being an integrin.
