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Title: Cloning and characterization of a cDNA coding for mouse placental alkaline phosphatase

Journal Article · · Proc. Natl. Acad. Sci. U.S.A.; (United States)

Mouse alkaline phosphatase 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.

Research Organization:
Institute for Cancer Research, Philadelphia, PA (USA)
OSTI ID:
7027188
Journal Information:
Proc. Natl. Acad. Sci. U.S.A.; (United States), Vol. 84:20
Country of Publication:
United States
Language:
English