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http://purl.uniprot.org/citations/3912261http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3912261http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3912261http://www.w3.org/2000/01/rdf-schema#comment"We have studied the synthesis, secretion, and processing of human growth hormone (hGH) in Escherichia coli transformed with plasmids engineered for the expression of hGH as a secreted product. In one plasmid, pPreHGH207-2, the coding sequence of the natural hGH precursor (pre-hGH) is placed under the control of the E. coli trp promoter. In a second plasmid, pAPH-1, a DNA fragment containing the E. coli alkaline phosphatase promoter and signal sequence codons is fused to the mature hGH coding sequence (pho-hGH). Most of the hGH was present in the osmotic shock fluids of E. coli cells containing either plasmid, indicating transport to the periplasmic space. Amino acid sequencing of the N termini of the pre-hGH and pho-hGH gene products revealed that both were processed correctly. Electrophoretic analysis of these polypeptides on reducing and nonreducing sodium dodecyl sulfate (SDS)-polyacrylamide (PA) gels indicates that periplasmic hGH is monomeric and contains the same two disulfide bonds as authentic hGH."xsd:string
http://purl.uniprot.org/citations/3912261http://purl.org/dc/terms/identifier"doi:10.1016/0378-1119(85)90319-1"xsd:string
http://purl.uniprot.org/citations/3912261http://purl.org/dc/terms/identifier"doi:10.1016/0378-1119(85)90319-1"xsd:string
http://purl.uniprot.org/citations/3912261http://purl.uniprot.org/core/author"Gray G.L."xsd:string
http://purl.uniprot.org/citations/3912261http://purl.uniprot.org/core/author"Gray G.L."xsd:string
http://purl.uniprot.org/citations/3912261http://purl.uniprot.org/core/author"Chang C.N."xsd:string
http://purl.uniprot.org/citations/3912261http://purl.uniprot.org/core/author"Chang C.N."xsd:string
http://purl.uniprot.org/citations/3912261http://purl.uniprot.org/core/author"Baldridge J.S."xsd:string
http://purl.uniprot.org/citations/3912261http://purl.uniprot.org/core/author"Baldridge J.S."xsd:string
http://purl.uniprot.org/citations/3912261http://purl.uniprot.org/core/author"Heyneker H.L."xsd:string
http://purl.uniprot.org/citations/3912261http://purl.uniprot.org/core/author"Heyneker H.L."xsd:string
http://purl.uniprot.org/citations/3912261http://purl.uniprot.org/core/author"McKeown K.S."xsd:string
http://purl.uniprot.org/citations/3912261http://purl.uniprot.org/core/author"McKeown K.S."xsd:string
http://purl.uniprot.org/citations/3912261http://purl.uniprot.org/core/date"1985"xsd:gYear
http://purl.uniprot.org/citations/3912261http://purl.uniprot.org/core/date"1985"xsd:gYear
http://purl.uniprot.org/citations/3912261http://purl.uniprot.org/core/name"Gene"xsd:string
http://purl.uniprot.org/citations/3912261http://purl.uniprot.org/core/name"Gene"xsd:string
http://purl.uniprot.org/citations/3912261http://purl.uniprot.org/core/pages"247-254"xsd:string
http://purl.uniprot.org/citations/3912261http://purl.uniprot.org/core/pages"247-254"xsd:string
http://purl.uniprot.org/citations/3912261http://purl.uniprot.org/core/title"Periplasmic production of correctly processed human growth hormone in Escherichia coli: natural and bacterial signal sequences are interchangeable."xsd:string
http://purl.uniprot.org/citations/3912261http://purl.uniprot.org/core/title"Periplasmic production of correctly processed human growth hormone in Escherichia coli: natural and bacterial signal sequences are interchangeable."xsd:string
http://purl.uniprot.org/citations/3912261http://purl.uniprot.org/core/volume"39"xsd:string
http://purl.uniprot.org/citations/3912261http://purl.uniprot.org/core/volume"39"xsd:string