Article
Optimization of the signal-sequence cleavage site for secretion from Bacillus subtilis of a 34-amino acid fragment of human parathyroid hormone.
Gene - 30 Jun 1991
Saunders C W, Pedroni J A, Monahan P M
Abstract excerpt
We have effected the secretion from Bacillus subtilis of a 34-amino acid (aa) fragment of human parathyroid hormone (PTH,1-34), using a Bacillus amyloliquefaciens neutral protease signal sequence. The secretion efficiency depended on the aa sequence near the signal-sequence cleavage site. We constructed a series of gene fusions encoding different pairs of aa between the signal sequence and PTH,1-34. There was a...
Topics
- Amino Acid Sequence
- Bacillus subtilis
- Base Sequence
- DNA
- Humans
- Molecular Sequence Data
- Mutation
- Parathyroid Hormone
- Protein Conformation
- Protein Processing, Post-Translational
- Protein Sorting Signals