Carriers of hemophilia can often be detected because their plasmas contain a disproportionately high concentration of antihemophilic factor, measured immunologically, compared with the titer of procoagulant antihemophilic factor.
Estimation of the titer of procoagulant antihemophilic factor (AHF) and the concentration of AHF-like antigens, as detected by heterologous antiserum, provides a method for diagnosis of the carrier state of classic hemophilia.
Mutations leading to hemophilia A by substitution of amino acids in coagulation factor VIII may provide important clues to the structure and function of this large and enigmatic protein.
Mutations leading to hemophilia A by substitution of amino acids in coagulation factor VIII may provide important clues to the structure and function of this large and enigmatic protein.
Molecular characterization of severe hemophilia A suggests that about half the mutations are not within the coding regions and splice junctions of the factor VIII gene.
Molecular characterization of mild-to-moderate hemophilia A: detection of the mutation in 25 of 29 patients by denaturing gradient gel electrophoresis.
Characterization of a thrombin cleavage site mutation (Arg 1689 to Cys) in the factor VIII gene of two unrelated patients with cross-reacting material-positive hemophilia A.
The diagnostic potential of a basal rate of transcription in non-expressing tissues was then demonstrated by the detection of a novel point mutation in the FVIII gene causing haemophilia A by PCR/direct sequencing of ectopically transcribed mRNA derived from patient lymphocytes.
The presence of gene lesions in coagulation factor VIII (FVIII) gene was investigated in 70 Italian patients severely affected by haemophilia A. cDNA probes specific for exons 14-26 of the FVIII gene were used.