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Administracin de cidos nucleicos que codifican polipptidos de FX modificados (terapia gnica) 3

Still, there remained the possibility that Fe-S cluster turnover exceeds the 20 h starvation timeframe used for these studies, which would negate the necessity of de novo synthesis

Disulfide bonds (RS SR) are more stable than peroxide bonds (RO OR) and this enhanced stability is a key advantage due to which disulfide bonds are integral part of the structural features of proteins

For example, the modified FX polypeptide is a modified zymogen FX containing substitution (s) of amino acids in a zymogen FX polypeptide containing a light chain having at least 80%, 85%, 86%, 87%, 88 %, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more sequence identity with the zymogen FX light chain polypeptide has the sequence of amino acids 1-139 of SEQ ID NO: 134 and / or a heavy chain having at least 80%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or more sequence identity with the zymogen FX heavy chain polypeptide having the amino acid sequence 143-448 of the SEQ ID NO: 134 Examples of said modified zymogen FX polypeptides are FX polypeptides containing a light chain having amino acid sequence 1-139 shown in ID NO: 134 (ie, corresponding to amino acids 1-139 of any of SEQ ID NOS