Fibrinogen Osaka IV: a congenital dysfibrinogenemia found in a patient originally reported in relation to surgery, now defined to have an A alpha arginine-16 to histidine substitution.
Surg Today
; 23(1): 45-50, 1993.
Article
in En
| MEDLINE
| ID: mdl-8461606
ABSTRACT
We discovered a congenital heterozygous dysfibrinogen in a patient and reported this case in relation to surgery some time ago (Jpn J Surg (1988) 1843-46). Further studies on the isolated abnormal population of fibrinogen derived from this patient have revealed that fibrinopeptide A was not cleaved by ancrod, a snake venom-derived thrombin-like enzyme, but by thrombin, slowly but completely. The released fibrinopeptide A components, being the A, AY, and AP peptides, were all found to be abnormal, as evidenced by slightly earlier elution positions on high-performance liquid chromatography, compared with the normal counterparts. By analyzing their amino acid sequence, we have identified an arginine to histidine substitution at position 16 of the A alpha chain, the thrombin cleavage site. Utilizing insolubilized abnormal fibrinogen, we confirmed that the polymerization site assigned to the central E domain, the "A" site, was exposed by thrombin, but not by ancrod. This dysfibrinogen, designated as fibrinogen Osaka IV, is the second abnormal molecule with an A alpha arginine-16 to histidine substitution identified among Japanese families.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Arginine
/
Fibrinogens, Abnormal
/
Afibrinogenemia
/
Histidine
Type of study:
Prognostic_studies
Limits:
Humans
/
Male
/
Middle aged
Language:
En
Journal:
Surg Today
Year:
1993
Document type:
Article
Affiliation country:
Japón