Question

classic haemophilia is an x-linked recessive disease. the gene encodes blood clotting factor viii. analysis of the dna sequences that encode factor viii showed that all members of an affected family have a particular point mutation. all have a mutation in amino acid position 282, resulting from a 5' cat 3' to 5' gat 3' change in exon 8. the mutation results in an amino acid change from: _______

Answer 1

The point mutation described for classic hemophilia results in an amino acid change from Histidine (His) to Aspartic acid (Asp) at position 282 due to a CAT to GAT substitution in the DNA sequence encoding for factor VIII.

Step-by-step explanation:

Classic hemophilia is an X-linked recessive disease characterized by the absence or malfunctioning of clotting factor VIII due to a genetic mutation. When analyzing the DNA sequences encoding factor VIII, a particular point mutation at amino acid position 282 is observed. This mutation is a change from 5' CAT 3' to 5' GAT 3' in exon 8, affecting the protein's structure. The amino acid change from CAT (which codes for Histidine, His) to GAT (which codes for Aspartic acid, Asp) directly impacts the blood clotting process and is responsible for the hemophilia phenotype observed in affected individuals.