| Title: | Expression and secretion of biologically active human atrial natriuretic peptide in Saccharomyces cerevisiae |
| Author(s): | Vlasuk GP; Bencen GH; Scarborough RM; Tsai PK; Whang JL; Maack T; Camargo MJ; Kirsher SW; Abraham JA; |
| ISSN/ISBN: | 0021-9258 (Print) 0021-9258 (Linking) |
| Abstract: | "A hybrid gene was constructed containing a fusion between the DNA sequences encoding the secretory precursor of the yeast mating pheromone alpha-factor and a synthetic sequence encoding a biologically active 24-amino acid carboxyl-terminal portion of the human atrial natriuretic peptide (hANP) precursor. Transformation of Saccharomyces cerevisiae with the hybrid gene resulted in the yeast cells secreting biologically active hANP into the extracellular medium. The secreted hANP was purified and found to be accurately processed at the junction in the chimeric alpha-factor/hANP protein, producing the desired mature hANP amino terminus. The secreted product was also folded correctly with respect to the single disulfide bond. However, the carboxyl terminus of the secreted hANP material was heterogeneous such that the major form lacked the last two amino acids of the peptide while the minor form was the full length material. The observed processing at the carboxyl terminus of the secreted hANP may reflect a normal processing event involved in alpha-factor peptide maturation" |
| Keywords: | "Amino Acid Sequence Atrial Natriuretic Factor/*genetics/metabolism Chromatography, High Pressure Liquid DNA, Recombinant Electrophoresis, Polyacrylamide Gel Escherichia coli/genetics Humans Peptide Fragments/genetics Plasmids Saccharomyces cerevisiae/*gen;" |
| Notes: | "MedlineVlasuk, G P Bencen, G H Scarborough, R M Tsai, P K Whang, J L Maack, T Camargo, M J Kirsher, S W Abraham, J A eng Research Support, Non-U.S. Gov't 1986/04/15 J Biol Chem. 1986 Apr 15; 261(11):4789-96" |
