Fibrinogen Kaiserslautern III: A new case of congenital dysfibrinogenemia with Aα 16 Arg → Cys substitution

Haemostasis

Volumn 31, Issue 1, 2001, Pages 12-17

  Loreth, Ralph M ^a   Meyer, M ^b   Albert, F W ^a  

^a Westpfalz Klinikum GmbH   (Germany)

^b FH Jena ^*  (Germany)

Author keywords

Bleeding tendency; Dysfibrinogenemia; Fibrinogen; Fibrinogen variant; Fibrinopeptide A; Mutation

Indexed keywords

BATROXOBIN; FIBRINOGEN; FIBRINOPEPTIDE A; FIBRINOPEPTIDE B; THROMBIN;

ADULT; AMINO ACID SUBSTITUTION; ARTICLE; BLEEDING TENDENCY; BLOOD CLOTTING TIME; CASE REPORT; DNA SEQUENCE; DYSFIBRINOGENEMIA; EXON; HUMAN; MALE; POINT MUTATION; PRIORITY JOURNAL; PROTHROMBIN TIME;

EID: 0034946866     PISSN: 03010147     EISSN: None     Source Type: Journal    
DOI: 10.1159/000048039     Document Type: Article

References (13)

1. Familial dysfibrinogenemia and thrombophilia: Report on a study of the SCC subcommittee on fibrinogen
2. Dysfibrinogenemia and other disorders of fibrinogen structure and function
3. Human fibrinogen - Structural variants and functional sites
4. Isolation of human fibrinogen of high purity and in high yield using polyethylene glycol 1000
5. Cleavage of structural proteins during the assembly of the head of bacteriophage T4
6. Fibrinogen and fibrin polymerization: Appraisal of the binding events that accompany fibrin generation and fibrin clot assembly
7. Thrombin-induced fibrinopeptide B release from normal and variant fibrinogens: Influence of inhibitors of fibrin polymerization
8. Detection of fibrinogen abnormality in dysfibrinogenemia: Special report of fibrinogen Metz characterized by an amino acid substitution located at the peptide bond cleaved by thrombin
9. Fibrinogen Bergamo I (Aα 16Arg → Cys): Susceptibility towards thrombin following aminoethylation, methylation or carboxamidomethylation of cysteine residues
10. Fibrinogens Kawaguchi and Osaka: An amino acid substitution of Aα arginine-16 to cysteine which forms an extra interchain disulfide bridge between the two Aα chains
11. Aspects of evaluation of fibrinogen Stony Brook: A defect resulting in failure to release peptide A
12. Fibrinogen Ledyard (Aα Arg16-Cys): Biochemical and physiologic characterization
13. Fibrinogen Bergamo III and fibrinogen Torino: Two further variants with hereditary molecular defects in fibrinopeptide A