Paolo Simioni.

Thus, it really is unlikely that mutation is normally a silent polymorphism. These findings implicate the R338L mutation as the reason behind the gain-of-function home of the mutant factor IX. Previously, Chang et al. Found that site-particular mutagenesis that substituted alanine for arginine at position 338 resulted in one factor IX molecule with clotting activity that was 3 x the clotting activity in wild-type factor IX.19 This region of the protein is essential for substrate binding, and changing from arginine to alanine at position 338 escalates the efficiency of the binding of the substrate to the enzyme .10 Sites at which cytosines precede a guanosine in the DNA sequence are believed to be hotspots for mutations,22 and mutations in CpG dinucleotides comprise 25 percent of all mutations in hemophilia B.15 Stop-codon mutations at R338 are normal in hemophilia B, but the anticipated rates of mutations due to transition at R338 are underrepresented.23 The only missense mutation at this position in hemophilia B is R338P.15..The dropout rate was reduced the groups that were designated to high-protein diets and the groups that were designated to low-glycemic-index diets than in the group that was assigned to the diet that was low in protein and had a higher glycemic index . The low-glycemic-index diets were associated with a lower risk of dropout than were the high-glycemic-index diets , and there is a craze toward a lower risk of drop-out with the high-protein diet programs than with the low-protein diets .