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A family with hereditary factor X deficiency with a point mutation Gla 32 to Gln in the Gla domain (factor X Tokyo)
Author(s) -
Zama Takeru,
Murata Mitsuru,
Watanabe Reiko,
Yokoyama Kenji,
Moriki Takanori,
Ambo Hironobu,
Murakami Hiroshi,
Kikuchi Masao,
Ikeda Yasuo
Publication year - 1999
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1046/j.1365-2141.1999.01614.x
Subject(s) - factor x , partial thromboplastin time , point mutation , factor ix , factor xi , mutation , clotting time , coagulopathy , thromboplastin , microbiology and biotechnology , factor v , medicine , genetics , biology , chemistry , coagulation , thrombin , gene , platelet , thrombosis
We report a new family with hereditary factor X deficiency. The propositus had a markedly prolonged prothrombin time, a mild prolongation of activated partial thromboplastin time and a clotting time activated by Russell's viper venom. Factor X activity in plasma was 3 u/dl (normal range 56–138 u/dl). Factor X antigen level was 61 u/dl. Molecular analysis revealed a homozygous mutation, Glu ( G AG) to Gln ( C AG) at residue 32 which normally undergoes γ‐carboxylation within the γ‐carboxyglutamic acid rich domain. The genotypes of family members completely correlated with their factor X activities. It is suggested that the Glu 32 to Gln mutation is the molecular basis for the abnormal factor X in this family.