Abstract
Enzymatic DNA amplification and complete sequence analysis were used to investigate human factor IX coding sequences in three CRM+ hemophilia B patients. In a patient with severe hemophilia B and a markedly prolonged ox-brain prothrombin time, a C to T transition in exon VI changed the codon for Arg180 to Trp (factor IX B(M)Nagoya 2). This mutation would impair the cleavage by factor XIa required for activation of the zymogen. In a patient with mild hemophilia B, a G to A transition in exon VI changed the codon for Arg145 to His (factor IX Nagoya 3). This substitution also would be predicted to preclude the cleavage of factor IX by factor XIa at this peptide bond (Arg145-Ala146). Furthermore, this point mutation creates a new NlaIII restriction site which provides a quick and reliable method for carrier detection in the affected family members. A patient with severe hemophilia B (factor IX Nagoya 4) had a G to A transition in exon II changing the codon for Glu21 to Lys. This novel point mutation is assumed to impair the function of factor IX by disrupting the calcium binding of factor IX.
| Original language | English |
|---|---|
| Pages (from-to) | 514-520 |
| Number of pages | 7 |
| Journal | Thrombosis and Haemostasis |
| Volume | 65 |
| Issue number | 5 |
| Publication status | Published - 1991 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Hematology
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Three distinct point mutations in the factor IX gene of three Japanese CRM+ hemophilia B patients (factor IX B(M)Nagoya 2, factor IX Nagoya 3 and 4). / Hamaguchi, M.; Matsushita, T.; Tanimoto, M.; Takahashi, I.; Yamamoto, K.; Sugiura, I.; Takamatsu, J.; Ogata, K.; Kamiya, T.; Saito, H.
In: Thrombosis and Haemostasis, Vol. 65, No. 5, 1991, p. 514-520.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Three distinct point mutations in the factor IX gene of three Japanese CRM+ hemophilia B patients (factor IX B(M)Nagoya 2, factor IX Nagoya 3 and 4)
AU - Hamaguchi, M.
AU - Matsushita, T.
AU - Tanimoto, M.
AU - Takahashi, I.
AU - Yamamoto, K.
AU - Sugiura, I.
AU - Takamatsu, J.
AU - Ogata, K.
AU - Kamiya, T.
AU - Saito, H.
PY - 1991
Y1 - 1991
N2 - Enzymatic DNA amplification and complete sequence analysis were used to investigate human factor IX coding sequences in three CRM+ hemophilia B patients. In a patient with severe hemophilia B and a markedly prolonged ox-brain prothrombin time, a C to T transition in exon VI changed the codon for Arg180 to Trp (factor IX B(M)Nagoya 2). This mutation would impair the cleavage by factor XIa required for activation of the zymogen. In a patient with mild hemophilia B, a G to A transition in exon VI changed the codon for Arg145 to His (factor IX Nagoya 3). This substitution also would be predicted to preclude the cleavage of factor IX by factor XIa at this peptide bond (Arg145-Ala146). Furthermore, this point mutation creates a new NlaIII restriction site which provides a quick and reliable method for carrier detection in the affected family members. A patient with severe hemophilia B (factor IX Nagoya 4) had a G to A transition in exon II changing the codon for Glu21 to Lys. This novel point mutation is assumed to impair the function of factor IX by disrupting the calcium binding of factor IX.
AB - Enzymatic DNA amplification and complete sequence analysis were used to investigate human factor IX coding sequences in three CRM+ hemophilia B patients. In a patient with severe hemophilia B and a markedly prolonged ox-brain prothrombin time, a C to T transition in exon VI changed the codon for Arg180 to Trp (factor IX B(M)Nagoya 2). This mutation would impair the cleavage by factor XIa required for activation of the zymogen. In a patient with mild hemophilia B, a G to A transition in exon VI changed the codon for Arg145 to His (factor IX Nagoya 3). This substitution also would be predicted to preclude the cleavage of factor IX by factor XIa at this peptide bond (Arg145-Ala146). Furthermore, this point mutation creates a new NlaIII restriction site which provides a quick and reliable method for carrier detection in the affected family members. A patient with severe hemophilia B (factor IX Nagoya 4) had a G to A transition in exon II changing the codon for Glu21 to Lys. This novel point mutation is assumed to impair the function of factor IX by disrupting the calcium binding of factor IX.
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M3 - Article
C2 - 1871712
AN - SCOPUS:0025904605
VL - 65
SP - 514
EP - 520
JO - Thrombosis and Haemostasis
JF - Thrombosis and Haemostasis
SN - 0340-6245
IS - 5
ER -