| First Author | Terao M | Year | 1987 |
| Journal | Proc Natl Acad Sci U S A | Volume | 84 |
| Issue | 20 | Pages | 7051-5 |
| PubMed ID | 3478679 | Mgi Jnum | J:8897 |
| Mgi Id | MGI:57362 | Doi | 10.1073/pnas.84.20.7051 |
| Citation | Terao M, et al. (1987) Cloning and characterization of a cDNA coding for mouse placental alkaline phosphatase. Proc Natl Acad Sci U S A 84(20):7051-5 |
| abstractText | 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. |
