SYNTHESIS AND SECRETION OF HUMAN ATRIAL NATRIURETIC PEPTIDE IN Saccharomyces cerevisiae

A chemically synthesized α-hANP gene was inserted into plasmid YFD18, which was an expression-secretion vector of yeast. The recombinant then transformed in the yeast Y33. The expression level of yeast transformants was about 700 μg ANP/L detected by RIA. More than 99% of expression products were secreted in the culture medium. N-terminal analysis of purified product showed that the first 4 amino acid residues of α-hANP were deleted.     

人心钠素在酵母细胞中的合成与分泌

将化学合成的人α心钠素基因插入酵母分泌表达载体YFD18,然后把重组质粒转化进酵母菌Y33.用放射免疫分析测得酵母转化子表达心钠素的水平约为700μg/1,其中有99％以上在培养液中.对纯化产物的N末端分析表明人α心钠素的前4个氨基酸残基被缺失了.