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In this video we explore the traditional way that synthetic, recombinant human insulin is produced, by synthesising the A and B chains separately in separate strains of E. coli, and then combined in vitro to make insulin. We look at how ampicillin and tetracycline resistance genes, and blue-white screening with X-gal are used to identify recombinant colonies, and the role of β-galactosidase in promoting transcription and as a reporter gene. We also look at the reason for creating fusion proteins, as a precursor to the final product, and other questions that are frequently asked about the process..
Images of proteins are generated from www.rcsb.org/3... and www.rcsb.org/3.... All other images © Andrew Douch. biologypodcast@gmail.com