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http://purl.uniprot.org/citations/2909511http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2909511http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2909511http://www.w3.org/2000/01/rdf-schema#comment"Dopamine beta-hydroxylase exists in bovine adrenal medulla chromaffin granules in both soluble and membrane-bound forms. The mechanism by which membranous dopamine beta-hydroxylase is bound to granule membranes has been elusive. Recently, evidence that covalently attached phosphatidylinositol does not serve as an anchor for membranous dopamine beta-hydroxylase was reported (Stewart, L. C., and Klinman, J. P. (1988) J. Biol. Chem. 263, 12183-12186). It was suggested that an uncleaved signal sequence could serve as a mode of attachment for the membrane-bound hydroxylase. Amino-terminal sequence analysis of purified bovine membranous dopamine beta-hydroxylase demonstrates that this form of the enzyme possesses an amino-terminal sequence similar to the soluble enzyme. Additionally, the 75- and 72-kDa bands of membranous dopamine beta-hydroxylase were electrophoretically eluted from a preparative sodium dodecyl sulfate-polyacrylamide gel and sequenced. Both bands had the amino-terminal sequence characteristic of the soluble bovine enzyme. These sequence results eliminate the possibility that an uncleaved signal sequence serves as the membrane anchor."xsd:string
http://purl.uniprot.org/citations/2909511http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(17)31216-4"xsd:string
http://purl.uniprot.org/citations/2909511http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(17)31216-4"xsd:string
http://purl.uniprot.org/citations/2909511http://purl.uniprot.org/core/author"Fleming P.J."xsd:string
http://purl.uniprot.org/citations/2909511http://purl.uniprot.org/core/author"Fleming P.J."xsd:string
http://purl.uniprot.org/citations/2909511http://purl.uniprot.org/core/author"Kent U.M."xsd:string
http://purl.uniprot.org/citations/2909511http://purl.uniprot.org/core/author"Kent U.M."xsd:string
http://purl.uniprot.org/citations/2909511http://purl.uniprot.org/core/author"Taylor C.S."xsd:string
http://purl.uniprot.org/citations/2909511http://purl.uniprot.org/core/author"Taylor C.S."xsd:string
http://purl.uniprot.org/citations/2909511http://purl.uniprot.org/core/date"1989"xsd:gYear
http://purl.uniprot.org/citations/2909511http://purl.uniprot.org/core/date"1989"xsd:gYear
http://purl.uniprot.org/citations/2909511http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/2909511http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/2909511http://purl.uniprot.org/core/pages"14-16"xsd:string
http://purl.uniprot.org/citations/2909511http://purl.uniprot.org/core/pages"14-16"xsd:string
http://purl.uniprot.org/citations/2909511http://purl.uniprot.org/core/title"The membrane-binding segment of dopamine beta-hydroxylase is not an uncleaved signal sequence."xsd:string
http://purl.uniprot.org/citations/2909511http://purl.uniprot.org/core/title"The membrane-binding segment of dopamine beta-hydroxylase is not an uncleaved signal sequence."xsd:string
http://purl.uniprot.org/citations/2909511http://purl.uniprot.org/core/volume"264"xsd:string
http://purl.uniprot.org/citations/2909511http://purl.uniprot.org/core/volume"264"xsd:string
http://purl.uniprot.org/citations/2909511http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2909511
http://purl.uniprot.org/citations/2909511http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2909511
http://purl.uniprot.org/citations/2909511http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/2909511
http://purl.uniprot.org/citations/2909511http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/2909511