A new mutation (Arg251Trp) in the Ca2+ binding site of factor X protease domain appears to be responsible for the defect in the extrinsic pathway activation of factor X Padua.
Clin Appl Thromb Hemost
; 10(1): 5-8, 2004 Jan.
Article
en En
| MEDLINE
| ID: mdl-14979399
Factor X Padua, first described a few years ago, is characterized by a defect only in the extrinsic system. In this present paper, the molecular basis for this peculiar defect is investigated. Polymerase chain reaction amplification and direct sequencing of the entire FX coding sequence and of exon-intron junctions detected in the proposita a C-to-T translocation in exon 8 of nucleotide 875 at the homozygous level. This resulted in the substitution of tryptophan for arginine 251. A niece of the proposita was shown to be heterozygous for the abnormality. Molecular modeling suggested that the mutation does not alter significantly folding and stability of the protein but may be involved in the Ca2+ binding site.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Trastornos de la Coagulación Sanguínea
/
Factor X
/
Mutación Missense
Tipo de estudio:
Prognostic_studies
Límite:
Female
/
Humans
/
Middle aged
Idioma:
En
Revista:
Clin Appl Thromb Hemost
Asunto de la revista:
ANGIOLOGIA
Año:
2004
Tipo del documento:
Article
País de afiliación:
Italia
Pais de publicación:
Estados Unidos