Abstract
A high yield of Escherichia coli outer membrane proteins OmpA (about 200 mg/l) and OmpF (about 100 mg/l) was obtained in Bacillus subtilis when produced intracellularly. The yield was more than 100-fold higher than the yield of these proteins by a similar vector containing the complete signal sequence of alpha-amylase of B. amyloliquefaciens. Both proteins isolated after breakage of the B. subtilis cells by low-speed centrifugation were about 70% pure and could be solubilized by Sarkosyl, SDS and guanidine hydrochloride.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacillus subtilis / genetics*
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Bacterial Outer Membrane Proteins / biosynthesis
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Bacterial Outer Membrane Proteins / genetics*
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Bacterial Outer Membrane Proteins / isolation & purification
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Cloning, Molecular
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DNA, Recombinant / metabolism
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Electrophoresis, Polyacrylamide Gel
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Escherichia coli / genetics*
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Molecular Sequence Data
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Plasmids
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / isolation & purification
Substances
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Bacterial Outer Membrane Proteins
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DNA, Recombinant
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Recombinant Proteins