Blood clotting factor IX niigata: Substitution of alanine-390 by valine in the catalytic domain

Mitsuhiko Sugimoto, Toshiyuki Miyata, Shun ichiro Kawabata, Akira Yoshioka, Hiromu Fukui, Hoyo Takahashi, Sadakki Iwanaga

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)

Abstract

Factor IX Niigata is a mutant factor IX responsible for the moderately severe hemophilia B in a patient who has a normal level of factor IX antigen with reduced clotting activity (1- 4% of normal). We reported previously that the purified mutant protein could be converted to the factor IXaβ form by factor XIa/Ca2+ at a rate similar to that in the case of normal factor IX, but the resulting mutant factor IXaβ could not activate factor X in the presence of factor VIII, Ca2+ and phospholipids (Yoshioka, A. et al. (1986) Thromb. Res. 42, 595-604). In the present study, we analyzed factor IX Niigata at the structural level to elucidate the molecular abnormality responsible for the loss of clotting activity. Amino acid sequence analysis of a peptide obtained on lysyl endopeptidase digestion, coupled with subsequent SP-V8 digestion, demonstrated that the alanine at position 390 was substituted by valine in the catalytic domain of the factor IX Niigata molecule.

Original languageEnglish
Pages (from-to)878-880
Number of pages3
JournalJournal of biochemistry
Volume104
Issue number6
DOIs
Publication statusPublished - Dec 1988

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

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