SUMMARY: mutants of K12 spontaneously released alkaline phosphatase (APase) into the extracellular medium to give up to 300 units ml. APase is a phosphate repressible periplasmic enzyme encoded by the gene . With a view to establishing a method of easy purification, we have analysed APase synthesis and release patterns of isogenic strains containing either a constitutive regulatory mutation, or a hybrid plasmid carrying the structural gene and regulatory genes, or a transducing ϕ 80 phage. In the presence of the mutation, F strains lysogenized with ϕ 80 phage and grown in high phosphate medium were able to release eight times more APase activity (2300 units ml) than haploid strain 2336 ( ) grown in low phosphate medium. Neither protein synthesis, the cell export machinery nor leakage mechanisms were limiting for APase release. Sufficient APase was released into the medium to facilitate its purification.


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