Abstract
The spore coat of Bacillus subtilis was isolated and solubilized by treatment with sodium dodecyl sulfate (SDS) plus dithiothreitol (DTT) solution. This treatment solubilized about 85% of the spore coat fraction and the soluble fraction mainly consisted of protein. The protein was purified in a buffer containing the detergent. The results of gel filtration, SDS-disc gel electrophoresis and NH2-terminal analysis showed the major component of the spore coat protein to be one kind with a molecular weight of 14, 000.
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