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Purification of Bacillus subtilis Spore Coat Protein by Electrophoretic Elution Procedure and Determination of NH 2 ‐Terminal Amino Acid Sequences
Author(s) -
Abe Akiko,
Ogawa Setsuko,
Kohno Takeyuki,
Watabe Kazuhito
Publication year - 1993
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1993.tb01709.x
Subject(s) - bacillus subtilis , biology , electrophoresis , coat , amino acid , molecular mass , spore , elution , biochemistry , gel electrophoresis , chromatography , bacillaceae , peptide sequence , microbiology and biotechnology , bacteria , chemistry , genetics , enzyme , gene , paleontology
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.