ISSN:
1432-072X
Keywords:
Cyanobacteria
;
Outer membrane
;
Peptidoglycan
;
associated protein
;
Pore-forming protein
;
Porin
;
Synechococcus
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract 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 52000. 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 45000 in contrast to the mobility on SDS-PAGE.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00276478
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