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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Partial purification of a cyanobacterial membrane protein with amino terminal sequence similarity to the N-methylphenylalanine pilins.

Cyanobacterial pilin was extracted from Synechococcus 6301 membranes using a detergent mixture comprising 1% Triton X-100, 1% Thesit and 0.5% dodecyl beta-D-maltoside. Partial purification of pilin from the crude extract was achieved by a single-step purification applying the Rotofor isoelectric focusing system. Up to 100-fold purification of pilin from the crude extract was achieved in a single run. SDS-PAGE analysis showed Synechococcus 6301 pilin migration with an apparent molecular weight of 11 kDa. The amino terminal sequence of the first 28 amino acid residues was identified. Alignment of the predicted sequence showed a 60-80% identity with amino terminal sequences of pilins from pathogenic gram-negative bacteria (enterobacteria). The apparent mass of Synechococcus 6301 pilin was, however, lower. The amino terminus of Synechococcus 6301 pilin, as with other pilins, has a high content of hydrophobic amino acids.[1]

References

  1. Partial purification of a cyanobacterial membrane protein with amino terminal sequence similarity to the N-methylphenylalanine pilins. Nore, B.F., Harrison, M.A., Keen, J.N., Allen, J.F. Acta Chem. Scand. (1994) [Pubmed]
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