Synthesis and secretion of wheat α-amylase in Saccharomyces cerevisiae
| Autor: | Anthony A. Gatenby, David C. Baulcombe, Kristine N. Lahners, Steven J. Rothstein, Colin M. Lazarus |
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| Rok vydání: | 1987 |
| Předmět: |
Signal peptide
Phosphoglycerate kinase Methionine biology Recombinant Fusion Proteins Saccharomyces cerevisiae General Medicine Protein Sorting Signals biology.organism_classification Recombinant Proteins Yeast Culture Media chemistry.chemical_compound Biochemistry chemistry Complementary DNA Genetics biology.protein Secretion Amylase alpha-Amylases Protein Processing Post-Translational Triticum Plant Proteins |
| Zdroj: | Gene. 55:353-356 |
| ISSN: | 0378-1119 |
| DOI: | 10.1016/0378-1119(87)90296-4 |
| Popis: | A wheat alpha-amylase cDNA clone has been fused to the phosphoglycerate kinase initiator methionine to enable synthesis in the yeast Saccharomyces cerevisiae of an alpha-amylase enzyme that is identical in size to the wild-type alpha-amylase. The alpha-amylase is synthesized with an N-terminal plant signal peptide which is recognized in the yeast host, leading to efficient processing and secretion into the medium. The secretion of alpha-amylase into the medium is quite efficient in rich medium, but barely detectable in a minimal medium. |
| Databáze: | OpenAIRE |
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