Expression and secretion of biologically active human atrial natriuretic peptide in Saccharomyces cerevisiae.

Vlasuk, George P.; Bencen, G H; Scarborough, Robert M.; Tsai, Pei‐Ju; Whang, J.L.; Maack, Thomas; Camargo, M. J. F.; Kirsher, Steven W.; Abraham, Judith A.

doi:10.1016/s0021-9258(19)89174-3

Cited by 53 publications

(1 citation statement)

References 28 publications

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“…Craig and Wondrack (1986) reported the presence of carboxypeptidase and aminopeptidase activity during the production of recombinant growth hormone releasing factor using a similar expression system. The presence of C-terminally degraded forms has also been reported by Vlasuk et al (1986) for secretion of recombinant human atrial natriuretic peptide from this expression system. These authors suggested that this processing may be due to an enzyme normally involved in the maturation of a-factor.…”

Section: Discussionsupporting

confidence: 54%

Purification and biochemical characterization of recombinant hirudin produced by Saccharomyces cerevisiae

Riehl-Bellon¹,

Carvallo²,

Acker³

et al. 1989

Biochemistry

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Recombinant hirudin was produced by the yeast Saccharomyces cerevisiae using the alpha-pheromone prepro sequence to direct its secretion into the culture medium. The secreted hirudin was isolated to greater than or equal to 95% purity as measured by 205-nm absorbance integration from a reverse-phase chromatogram. One major activity peak corresponding to the complete, correctly processed molecule and two minor activity peaks corresponding to C-terminally truncated forms were identified. The primary structure of the major peak, determined by N-terminal sequencing of tryptic peptides, was that predicted from the cDNA sequence, and the molecular mass analyzed by fast atom bombardment mass spectrometry (FAB-MS) was 6892.6 (calculated 6892.5). UV spectral analysis suggested that, in contrast to the natural molecule, recombinant hirudin produced by S. cerevisiae is not sulfated.

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Section: Discussionsupporting

confidence: 54%