The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II

Masanori Matsumoto, Yoshihiko Sakurai, Tetsuro Kokubo, Hideo Yagi, Kaori Makita, Taei Matsui, Koiti Titani, Yoshihiro Fujimura, Nobuhiro Narita

研究成果: Article査読

17 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)335-340
ページ数6
ジャーナルFEBS Letters
453
3
DOI
出版ステータスPublished - 25-06-1999

All Science Journal Classification (ASJC) codes

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学
  • 遺伝学
  • 細胞生物学

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