UMMS Affiliation

Department of Microbiology; Department of Microbiology and Physiological Systems

Publication Date


Document Type



Bacteriology | Biochemistry, Biophysics, and Structural Biology | Physiology


Extensively washed, dormant spores of Bacillus subtilis were disrupted with glass beads in buffer at pH 7 in the presence of protease inhibitors. Approximately 31% of the total spore protein was soluble, and another 14% was removed from the insoluble fraction by hydrolysis with lysozyme and washing with 1 M KCl and 0.1% sodium dodecyl sulfate. The residual spore integuments comprised 55% of the total spore proteins and consisted of coats and residual membrane components. Treatment of integuments with sodium dodecyl sulfate and reducing agents at pH 10 solubilized 40% of the total spore protein. Seven low-molecular-weight polypeptide components of this solubilized fraction comprised 27% of the total spore protein. They are not normal membrane components and reassociated to form fibrillar structures resembling spore coat fragments. The residual insoluble material (15% of the total spore protein) was rich in cysteine and was probably also derived from the spore coats. A solubilized coat polypeptide of molecular weight 12,200 has been purified in good yield (4 to 5% of the total spore protein). Five amino acids account for 92% of its total amino acid residues: glycine, 19%; tyrosine, 31%; proline, 23%; arginine, 13%; and phenylalanine, 6%.


Bacillus subtilis, spore, protein

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Copyright © 1978, American Society for Microbiology. Publisher PDF posted as allowed by the publisher's copyright policy at


J Bacteriol. 1978 Sep;135(3):1091-106. Link to article on publisher's website

Journal/Book/Conference Title

Journal of bacteriology

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Link to Article in PubMed

PubMed ID