Isolation, molecular characterization, and tissue-specific expression of ECP-51 and ECP-54 (TIP49), two homologous, interacting erythroid cytosolic proteins
U Salzer, M Kubicek, R Prohaska - Biochimica et Biophysica Acta (BBA) …, 1999 - Elsevier
We isolated two proteins, ECP-51 and ECP-54, from human erythrocyte cytosol by affinity
chromatography using a peptide of the integral membrane protein stomatin as bait. Partial
amino acid sequence information obtained by microsequencing allowed us to clone the
respective cDNAs. Analysis of the nucleotide sequences revealed that ECP-51 and ECP-54
are homologous (44.2% amino acid identity) and contain ATP-binding sites. ECP-54 was
identified as TIP49/RUVBL1/NMP238, which is a component of a large nuclear protein …
chromatography using a peptide of the integral membrane protein stomatin as bait. Partial
amino acid sequence information obtained by microsequencing allowed us to clone the
respective cDNAs. Analysis of the nucleotide sequences revealed that ECP-51 and ECP-54
are homologous (44.2% amino acid identity) and contain ATP-binding sites. ECP-54 was
identified as TIP49/RUVBL1/NMP238, which is a component of a large nuclear protein …