Abstract
To improve the secretion level of recombinant protein, the gene sequence coded the chicken lysozyme signal peptide (CLSP) connected with human lysozyme (HLY) was altered to substitute the amino acid sequence, and the effect of mutations on secretion of HLY in yeast was elucidated. The effect of mutations on secretion of recombinant HLY was elucidated in yeast. As the result of experiments, it has been shown that the positive charge in the N-terminal region of signal peptide plays an important role in the function of the eukaryotic signal peptide as well as that of prokaryote. This result enable us to design the ideal sequence for effective secretion of recombinant protein. Using such signal sequence containing additional Arginine residues, secretion levels of HLY in yeast were notably increased.
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