Synthesis and secretion of human atrial natriuretic peptide in Saccharomyces cerevisiae

Sci China B. 1991 Dec;34(12):1478-84.

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.

MeSH terms

  • Amino Acid Sequence
  • Atrial Natriuretic Factor / biosynthesis*
  • Atrial Natriuretic Factor / genetics
  • Cloning, Molecular
  • Escherichia coli / genetics
  • Genes
  • Molecular Sequence Data
  • Plasmids
  • Recombination, Genetic
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*

Substances

  • Atrial Natriuretic Factor