Alkaline Phosphatase Fusions: A Tag to Identify Mutations that Result in Increased Expression of Secreted Human Growth Hormone from Escherichia ... View Full Text


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Article Info

DATE

1986-01

AUTHORS

Mark Matteucci, Holly Lipetsky

ABSTRACT

We describe a method for the mutagenesis of a signal sequence, and the identification of mutations leading to the enhanced expression of periplasmicly secreted human growth hormone (HGH) from Escherichia coli. A plasmid was engineered, using deoxyoligonucleotide directed site specific mutagenesis, to contain two unique restriction sites flanking the signal sequence for HGH. The signal was mutagenized specifically using nitrous acid. Mutants resulting in enhanced expression of secreted HGH were detected by expressing and secreting a human growth hormone–alkaline phosphatase fusion protein possessing phosphatase activity. Such fusions show activity only when secreted. The signal sequence mutations isolated were transferred into plasmids directing the expression and secretion of native HGH and the phenotypes of enhanced expression of secreted protein were largely preserved. More... »

PAGES

51

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nbt0186-51

DOI

http://dx.doi.org/10.1038/nbt0186-51

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1051889302


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