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http://purl.uniprot.org/citations/2830166http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2830166http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2830166http://www.w3.org/2000/01/rdf-schema#comment"The expression and secretion of Bacillus amyloliquefaciens alpha-amylase was studied in yeast Saccharomyces cerevisiae. The Bacillus promoter was removed by BAL 31 digestion and three forms of the alpha-amylase gene were constructed: the Bacillus signal sequence was either complete (YEp alpha a1), partial (YEp alpha a2) or missing (YEp alpha a3). Secretion of alpha-amylase into the culture medium was obtained with the complete signal sequence only. The secreted alpha-amylase was glycosylated and its signal peptide was apparently processed. The glycosylated alpha-amylase remained active. The enzyme produced by the other constructions was not glycosylated and thus probably remained in the cytoplasm."xsd:string
http://purl.uniprot.org/citations/2830166http://purl.org/dc/terms/identifier"doi:10.1016/0378-1119(87)90324-6"xsd:string
http://purl.uniprot.org/citations/2830166http://purl.org/dc/terms/identifier"doi:10.1016/0378-1119(87)90324-6"xsd:string
http://purl.uniprot.org/citations/2830166http://purl.uniprot.org/core/author"Hackman P."xsd:string
http://purl.uniprot.org/citations/2830166http://purl.uniprot.org/core/author"Hackman P."xsd:string
http://purl.uniprot.org/citations/2830166http://purl.uniprot.org/core/author"Karaenen S."xsd:string
http://purl.uniprot.org/citations/2830166http://purl.uniprot.org/core/author"Karaenen S."xsd:string
http://purl.uniprot.org/citations/2830166http://purl.uniprot.org/core/author"Knowles J.K.C."xsd:string
http://purl.uniprot.org/citations/2830166http://purl.uniprot.org/core/author"Knowles J.K.C."xsd:string
http://purl.uniprot.org/citations/2830166http://purl.uniprot.org/core/author"Lehtovaara P."xsd:string
http://purl.uniprot.org/citations/2830166http://purl.uniprot.org/core/author"Lehtovaara P."xsd:string
http://purl.uniprot.org/citations/2830166http://purl.uniprot.org/core/author"Ruohonen L."xsd:string
http://purl.uniprot.org/citations/2830166http://purl.uniprot.org/core/author"Ruohonen L."xsd:string
http://purl.uniprot.org/citations/2830166http://purl.uniprot.org/core/date"1987"xsd:gYear
http://purl.uniprot.org/citations/2830166http://purl.uniprot.org/core/date"1987"xsd:gYear
http://purl.uniprot.org/citations/2830166http://purl.uniprot.org/core/name"Gene"xsd:string
http://purl.uniprot.org/citations/2830166http://purl.uniprot.org/core/name"Gene"xsd:string
http://purl.uniprot.org/citations/2830166http://purl.uniprot.org/core/pages"161-170"xsd:string
http://purl.uniprot.org/citations/2830166http://purl.uniprot.org/core/pages"161-170"xsd:string
http://purl.uniprot.org/citations/2830166http://purl.uniprot.org/core/title"Efficient secretion of Bacillus amyloliquefaciens alpha-amylase by its own signal peptide from Saccharomyces cerevisiae host cells."xsd:string
http://purl.uniprot.org/citations/2830166http://purl.uniprot.org/core/title"Efficient secretion of Bacillus amyloliquefaciens alpha-amylase by its own signal peptide from Saccharomyces cerevisiae host cells."xsd:string
http://purl.uniprot.org/citations/2830166http://purl.uniprot.org/core/volume"59"xsd:string
http://purl.uniprot.org/citations/2830166http://purl.uniprot.org/core/volume"59"xsd:string