Isolation and characterisation of porin from the outer membrane of Synechococcus PCC 6301

Pore-forming protein (porin) was isolated from N,N-dimethyl-dodecylaminoxid (LDAO)-extracted outer membranes of Synechococcus PCC 6301 and purified by ion exchange chromatography on DEAE-Sephacel column. The apparent molecular mass on SDS-PAGE was determined to be about 52,000. The native porin was...

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Bibliographic Details
Published in:Archives of microbiology 1994, Vol.161 (2), p.163-167
Main Authors: HANSEL, A, SCHMID, A, TADROS, M. H, JÜRGENS, U. J
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino Acids - analysis
Bacteriology
Biological and medical sciences
Cell Membrane - chemistry
Cyanobacteria - chemistry
Cyanobacteria - ultrastructure
Fundamental and applied biological sciences. Psychology
Ion Channels - analysis
Lipid Bilayers
Microbiology
Molecular Sequence Data
Molecular Weight
Permeability, membrane transport, intracellular transport
Porins - analysis
Porins - chemistry
Sequence Analysis
Synechococcus
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Summary:Pore-forming protein (porin) was isolated from N,N-dimethyl-dodecylaminoxid (LDAO)-extracted outer membranes of Synechococcus PCC 6301 and purified by ion exchange chromatography on DEAE-Sephacel column. The apparent molecular mass on SDS-PAGE was determined to be about 52,000. The native porin was reconstituted into black lipid bilayer membranes and showed a single-channel conductance of 5.5 nS in 1 M KCl. The porin was found to be N-terminally blocked. The C-terminal amino acid sequence was identified as Phe-Thr-Phe. Amino acid analysis suggested that the porin protein consists of about 420 amino acid residues, yielding a polarity of 43.6% and a molecular mass of 45,000 in contrast to the mobility on SDS-PAGE.
ISSN:0302-8933
1432-072X
DOI:10.1007/BF00276478