Isolation and characterization of an outer membrane protein of Chlorobium tepidum

被引：6

作者：

Aivaliotis, M

Neofotistou, E

Rémigy, HW

Tsimpinos, G

Lustig, A

Lottspeich, F

Tsiotis, G ^{[1
]}

机构：

[1] Univ Crete, Dept Chem, Div Biochem, Iraklion 71409, Greece

[2] Univ Basel, Bioctr, CH-4056 Basel, Switzerland

[3] Max Planck Inst Biochem, D-82152 Martinsried, Germany

来源：

PHOTOSYNTHESIS RESEARCH | 2004年 / 79卷 / 02期

关键词：

amino acid sequence; Chlorobium tepidum; outer membrane protein; protein digestion;

D O I：

10.1023/B:PRES.0000015383.58680.56

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

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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收藏

页码：161 / 166

页数：6

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