title: Synthesis and secretion of human atrial natriuretic peptide in Saccharomyces cerevisiae.
abstract: A chemically synthesized alpha-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 micrograms 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 alpha-hANP were deleted.
authors.affiliation: Institute of Genetics, Fudan University, Shanghai, PRC.
authors.forename: N
authors.initials: N
authors.lastname: Qin
authors.forename: N
authors.initials: N
authors.lastname: Wei
authors.forename: X H
authors.initials: XH
authors.lastname: Yao
authors.forename: Y Y
authors.initials: YY
authors.lastname: Li
mesh_terms: D000595:Amino Acid Sequence; D009320:Atrial Natriuretic Factor / Q000096:biosynthesis* / Q000235:genetics; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D005796:Genes; D008969:Molecular Sequence Data; D010957:Plasmids; D011995:Recombination, Genetic; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*
chemical_list: D009320:Atrial Natriuretic Factor