Studies of some physico-chemical and catalytic properties of hypoxanthine guanine phosphoribosyl transferase HGPRT) in thrombocytes of donors and patients with hemophilia A showed that kinetic parameters (Km, Vmax) of the enzyme were similar both under normal and pathological conditions. However, some differences were detected in thermolability and inhibition of HGPRT by purine metabolites: IMP, GMP and inosine. These data suggest that molecular impairment may occur in HGPRT under conditions of hemophilia A.
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