Evidence for two structural genes for alkaline phosphatase in Bacillus subtilis.

摘要: Two secreted alkaline phosphatase proteins were purified from cultures of Bacillus subtilis JH646MS. The two showed slight differences in subunit molecular weight, substrate specificity, and charge characteristics. A total 62% the first 22 amino-terminal amino acids identical. Both sequences conservation structural features identified Escherichia coli human phosphatases. One was a monomer other dimer. Southern analysis genomic DNA with degenerative oligomers based on acid suggest that there are genes for genome B. subtilis.