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Isolation and Characterization of an Outer Membrane Protein of Chlorobium tepidum
- Aivaliotis, Michalis, Neofotistou, Elefteria, Rémigy, Hervé-W., Tsimpinos, Georgios, Lustig, Ariel, Lottspeich, Friedrich, Tsiotis, Georgios
- Photosynthesis research 2004 v.79 no.2 pp. 161-166
- Chlorobium tepidum, agglutinins, amino acid composition, amino acids, bacteria, cyanogen, gel chromatography, high performance liquid chromatography, molecular weight, outer membrane proteins, polyacrylamide gel electrophoresis, sulfur, trypsin, ultracentrifugation
- A protein was isolated from membranes of the green sulfur bacterium Chlorobium tepidum. This protein was characterized by gel electrophoresis, gel filtration, analytical ultracentrifugation and amino acid sequencing. The molecular weight of the purified protein was shown to be 26 kDa by SDS-PAGE. HPLC gelfiltration, SDS-PAGE and analytical ultracentrifugation are consistent with the presence of a homogenous protein in the preparations. Amino acid analysis was obtained from the isolated protein after fragmentation with Lys-C, trypsin and cyanogen bromide. The cleavage pattern resulting from these treatments combined with Edman sequencing yield a sequence allowing the identification of an integral membrane agglutinin in Chl. tepidum.