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. HP...

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Published inPhotosynthesis research Vol. 79; no. 2; pp. 161 - 166
Main Authors Aivaliotis, Michalis, Neofotistou, Elefteria, Rémigy, Hervé-W, Tsimpinos, Georgios, Lustig, Ariel, Lottspeich, Friedrich, Tsiotis, Georgios
Format Journal Article
LanguageEnglish
Published Netherlands Springer Nature B.V 01.02.2004
Subjects
Proteins
protein digestion
amino acid sequence
Chlorobium tepidum
outer membrane protein
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Summary: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.
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ISSN:0166-8595
1573-5079
DOI:10.1023/B:PRES.0000015383.58680.56