title: Processing and secretion of human growth hormone with an artificial signal sequence.
abstract: We examined the secretion of human growth hormone in yeast cells with the artificial signal sequence L8LP, which is functional for human lysozyme secretion. The precursor was cleaved efficiently and the mature protein was secreted into the periplasmic space, but the protein aggregated. These results suggest that L8LP is also functional for human growth hormone. pI precipitation might be responsible for the aggregation.
authors.affiliation: Protein Engineering Research Institute, Osaka, Japan.
authors.forename: A
authors.initials: A
authors.lastname: Kohara
authors.forename: Y
authors.initials: Y
authors.lastname: Yamamoto
authors.forename: M
authors.initials: M
authors.lastname: Kikuchi
mesh_terms: D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D013006:Growth Hormone / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016296:Mutagenesis; D010957:Plasmids; D011487:Protein Conformation; D011498:Protein Precursors / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D021382:Protein Sorting Signals / Q000235:genetics* / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics
chemical_list: D011498:Protein Precursors; D021382:Protein Sorting Signals; D011994:Recombinant Proteins; D013006:Growth Hormone