| Literature DB >> 2105301 |
F M Hulett1, C Bookstein, K Jensen.
Abstract
Two secreted alkaline phosphatase proteins were purified from cultures of Bacillus subtilis JH646MS. The two proteins showed slight differences in subunit molecular weight, substrate specificity, and charge characteristics. A total of 62% of the first 22 amino-terminal amino acids were identical. Both sequences showed conservation of structural features identified in Escherichia coli and human alkaline phosphatases. One alkaline phosphatase was a monomer and the other was a dimer. Southern analysis of genomic DNA with degenerative oligomers based on the amino acid sequences suggest that there are two structural genes for alkaline phosphatase in the genome of B. subtilis.Entities:
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Year: 1990 PMID: 2105301 PMCID: PMC208500 DOI: 10.1128/jb.172.2.735-740.1990
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490