Three Abnormal Fibrinogen Variants with the Same Amino Acid Substitution (γ 275 Arg → His): Fibrinogens Bergamo II, Essen and Perugia
| Autor: | Agnes Henschen, T Barbui, H Kaudewitz, Eugene A. Beck, P Hilgard, G G Nenci, P Reber, M. Berrettini, Miha Furlan |
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| Rok vydání: | 1986 |
| Předmět: | |
| Zdroj: | Thrombosis and Haemostasis. 56:401-406 |
| ISSN: | 2567-689X 0340-6245 |
| Popis: | SummaryWe report on three unrelated individuals with the same uncommon type of dysfibrinogenemia, originating from Bergamo, Essen and Perugia. None of them showed bleeding symptoms while the Bergamo patient and members of her family presented with a thrombotic tendency. The presence of a defective fibrinogen was suggested by prolonged thrombin and rep-tilase times. Furthermore, fibrinogen concentrations of less than 0.28 g/L were determined by the functional assay whereas values of 1.5-2.4 g/L were measured by heat precipitation or electroimmunoassay. Fibrinogen was isolated by affinity chromatography on insoluble fibrin monomer. The rate of fibrinopeptide release by thrombin was normal while the fibrin polymerization reaction was strongly delayed. An abnormal peptide (γ265-310) was isolated by high-performance liquid chromatography after cyanogen bromide cleavage of the purified γ-chain of fibrinogen Bergamo II and Essen. The same peptide was also isolated following cyanogen bromide treatment of the intact fibrinogen Perugia. Sequence analyses of these peptides demonstrated the same amino acid exchange in all three fibrinogens: γ275 arginine → histidine. The described fibrinogen variants appear to possess a molecular defect which has thus far only been observed in fibrinogen Haifa. |
| Databáze: | OpenAIRE |
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