| 摘要 |
PURPOSE: To obtain the synthetic gene useful for industrially producing human myoglobin by using the optimal codon of E. coli, introducing restriction enzyme sites for cloning to both the ends of the obtained gene sequence, and subsequently secretion-expressing the holo type human heme myoglobin in the E. coli. CONSTITUTION: The gene sequence of human myoglobin is designed with the optimal codon of E. coli, and restriction enzyme sites (EcoRI-BamHI) for cloning are introduced to both the ends of the designed gene sequence to obtain the gene of the formula having a whole length of 484 base pairs. The gene is prepared by a chemical synthetic method, and subsequently inserted into an expression vector pTRP. E. coli JM109 is transformed with the treated vector and simultaneously cultured to produce the holo type human myoglobin in cytoplasm. |
