Purification of Bacillus subtilis spore coat protein by electrophoretic elution procedure and determination of NH2-terminal amino acid sequences.
Spore coat protein of Bacillus subtilis was purified by electrophoretic elution procedure. Solubilized coat protein components were separated on SDS-PAGE and the desired protein was recovered from the gel pieces under the optimal condition examined. Two purified polypeptides with molecular weights of about 40 kDa were obtained; each of them was in very closed size on SDS-PAGE, both retaining antigenic activity against anti-spore coat protein serum on immunoblot analysis. The N-terminal 23 and 30 amino acid sequences of them were determined, and they were not identical to each other and also not homologous in the sequences of coat proteins previously reported.
Abe
A
A
Faculty of Pharmaceutical Sciences, Setsunan University, Osaka, Japan.
Ogawa
S
S
Kohno
T
T
Watabe
K
K
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification*; D015139:Blotting, Southern; D004586:Electrophoresis; D015698:Genomic Library; D015151:Immunoblotting; D008969:Molecular Sequence Data; D012808:Sigma Factor; D013171:Spores, Bacterial / Q000737:chemistry*; D014157:Transcription Factors
D001426:Bacterial Proteins; D012808:Sigma Factor; D014157:Transcription Factors; C092468:spoIIR protein, Bacillus subtilis; C030069:spore-specific proteins, Bacillus