Blood clotting factor IX Nagoya 3: the molecular defect of zymogen activation caused by an arginine-145 to histidine substitution.

Abstract:

:Factor IX Nagoya 3 (IX Nagoya 3) is a natural mutant of factor IX recognized in a patient with moderately severe hemophilia B. The patient had 0.60 units/ml of factor IX antigen and 2-5% of clotting activity. IX Nagoya 3 was purified from the patient's plasma by immunoaffinity chromatography with an anti-factor IX monoclonal antibody column. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed that the treatment of IX Nagoya 3 with factor XIa/calcium ions resulted in cleavage only at the Arg180-Val181 bond. The amino acid sequence analysis of one of the lysyl endopeptidase peptides derived from IX Nagoya 3 revealed that Arg-145 is replaced by His. This substitution impairs the cleavage between the light chain and the activation peptide by factor XIa/calcium ions.

journal_name

Thromb Res

journal_title

Thrombosis research

authors

Suehiro K,Miyata T,Takeya H,Takamatsu J,Saito H,Murakawa M,Okamura T,Niho Y,Iwanaga S

doi

10.1016/0049-3848(90)90109-p

subject

Has Abstract

pub_date

1990-11-15 00:00:00

pages

311-20

issue

4

eissn

0049-3848

issn

1879-2472

journal_volume

60

pub_type

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