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) 18:43–46).3 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 Aα 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 Aα arginine-16 to histidine substitution identified among Japanese families.
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Yamazumi, K., Terukina, S., Matsuda, M. et al. Fibrinogen osaka IV: A congenital dysfibrinogenemia found in a patient originally reported in relation to surgery, now defined to have an Aα arginine-16 to histidine substitution. Surg Today 23, 45–50 (1993). https://doi.org/10.1007/BF00308999
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DOI: https://doi.org/10.1007/BF00308999