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• W2017991524 abstract "Mouse alkaline phosphatase [ALP; orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1] was partially purified from placenta. Data obtained by immunoblotting analysis suggested that the primary structure of this enzyme has a much greater homology to that of human and bovine liver ALPs than to the human placental isozyme. Therefore, a full-length cDNA encoding human liver-type ALP was used as a probe to isolate the mouse placental ALP cDNA. The cloned mouse cDNA is 2459 base pairs long and is composed of an open reading frame encoding a 524-amino acid polypeptide that contains a putative signal peptide of 17 amino acids. Homology at the amino acid level of the mouse placental ALP is 90% to the human liver isozyme but only 55% to the human placental counterpart. RNA blot hybridization results indicate that the mouse placental ALP is encoded by a gene identical to the gene expressed in mouse liver, kidney, and teratocarcinoma stem cells. This gene is therefore evolutionarily highly conserved in mouse and human." @default.
• W2017991524 created "2016-06-24" @default.
• W2017991524 creator A5013030326 @default.
• W2017991524 creator A5056182213 @default.
• W2017991524 date "1987-10-01" @default.
• W2017991524 modified "2023-10-03" @default.
• W2017991524 title "Cloning and characterization of a cDNA coding for mouse placental alkaline phosphatase." @default.
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• W2017991524 doi "https://doi.org/10.1073/pnas.84.20.7051" @default.
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