SUMMARY: The α-amylase structural gene () lacking its own signal peptide coding sequence was joined to the end of the alkaline phosphatase () signal peptide coding sequence by using the technique of oligonucleotide-directed site-specific deletion. On induction of the promoter, the α-amylase was expressed and almost all the activity was found in the periplasmic space of . The sequence of the five amino-terminal amino acids of the secreted polypeptide was Glu-Thr-Ala-Asn-Lys-, and thus the fused protein was correctly processed by the signal peptidase at the end of the signal peptide.


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