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The cDNA cloning of human placental ecto‐ATP diphosphohydrolases I and II 1
Author(s) -
Matsumoto Masanori,
Sakurai Yoshihiko,
Kokubo Tetsuro,
Yagi Hideo,
Makita Kaori,
Matsui Taei,
Titani Koiti,
Fujimura Yoshihiro,
Narita Nobuhiro
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00751-6
Subject(s) - complementary dna , enzyme , nucleotide , biochemistry , peptide sequence , nucleic acid sequence , biology , microbiology and biotechnology , amino acid , gene
The cDNA clones of two isoforms (enzymes I and II) of human placental ecto‐ATP diphosphohydrolases have been isolated based on the N‐terminal amino acid (aa) sequence of the immunopurified 82 kDa protein and characterized. The cDNA clone encoding enzyme I consists of 2081 nucleotides and the predicted enzyme I consists of 517 aa residues. Enzyme I has a 5′‐UTR and an N‐terminal 11 aa sequence that differ from CD39, but the rest of the sequence is the same as CD39. The hydropathy plot indicated that enzyme I has two hydrophobic regions near the N‐ and C‐termini of the molecule. In contrast, enzyme II consists of 1814 nucleotides and the predicted protein consists of 306 aa residues. The sequence of 1–1018 nucleotides of enzyme II is identical to that of enzyme I, but the 1019–1814 nucleotide sequence is different from both enzyme I and CD39. The hydropathy plot indicated that enzyme II has one hydrophobic region near the N‐terminus, suggesting that enzyme II is also anchored to the cell membrane. It is, however, likely that some of enzyme II exists as a soluble form in plasma, possibly after proteolytic processing.