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    Biochim Biophys Acta. 1991 Dec 2;1129(1):135-8.

    Cloning and sequence analysis of membrane-bound alkaline phosphatase cDNA of the silkworm, Bombyx mori.

    Itoh M, Takeda S, Yamamoto H, Izumi S, Tomino S, Eguchi M.

    Department of Applied Biology, Kyoto Institute of Technology, Japan.

    The nucleotide sequence (1974 bp) of cDNA coding for membrane-bound alkaline phosphatases (m-ALP) of Bombyx mori was isolated. The cDNA clone contained an open reading frame encoding a polypeptide (547 amino acids), which contains a hydrophobic signal peptide of 36 amino acids and the mature protein of 511 amino acids (Mr = 56,163). We found a highly hydrophobic domain presumed to be a membrane anchoring region at the C-terminus. Comparing analysis between Bombyx m-ALP and mammalian and Escherichia coli ALPs suggested an evolutionary relationship of sharing a common ancestral gene.

    PMID: 1756175 [PubMed - indexed for MEDLINE]

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