Isolation and Characterization of an Outer Membrane Protein of Chlorobium tepidum.
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.
Aivaliotis
Michalis
M
Department of Chemistry, Division of Biochemistry, University of Crete, Leoforos Knossou, 71409, Heraklion, Greece.
Neofotistou
Elefteria
E
Department of Chemistry, Division of Biochemistry, University of Crete, Leoforos Knossou, 71409, Heraklion, Greece.
Rémigy
Hervé-W
HW
Department of Chemistry, Division of Biochemistry, University of Crete, Leoforos Knossou, 71409, Heraklion, Greece.|Biozentrum, University of Basel, Klingelbergstr. 70, 4056, Basel, Switzerland.
Tsimpinos
Georgios
G
Department of Chemistry, Division of Biochemistry, University of Crete, Leoforos Knossou, 71409, Heraklion, Greece.
Lustig
Ariel
A
Biozentrum, University of Basel, Klingelbergstr. 70, 4056, Basel, Switzerland.
Lottspeich
Friedrich
F
Max Planck Institute for Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany.
Tsiotis
Georgios
G
Department of Chemistry, Division of Biochemistry, University of Crete, Leoforos Knossou, 71409, Heraklion, Greece.