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http://purl.uniprot.org/citations/6952938http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/6952938http://www.w3.org/2000/01/rdf-schema#comment"Phosphate incorporation from [gamma-32P]ATP into native and dephosphorylated alpha s1-casein is catalyzed by a casein kinase localized in the Golgi apparatus of lactating bovine mammary gland. Casein kinase from the Golgi is activated with either Mg2+ or Ca2+, and increased specific activity is observed with dephosphorylated casein as the substrate. The casein kinase can be solubilized from Golgi apparatus by the non-ionic detergent, Triton X-100. Gel permeation chromatography on Sepharose CL-4B yields a Stokes radius of 10 nm for the detergent-solubilized casein kinase. Dephosphorylated beta-peptide, the amino-terminal peptide from beta-casein, is a good substrate for the solubilized casein kinase. With dephosphorylated beta-peptide, the maximal velocity is 9.1 and 12.0 nmol/min per mg protein with Mg2+ and Ca2+ activation, respectively. The Michaelis constant for beta-peptide is greater with Ca2+ than with Mg2+ (4.8 mg/ml compared to 0.97 mg/ml). However, the Michaelis constant for ATP is not greatly influenced by these metal ions. The Triton X-100-solubilized Golgi enzyme can also catalyze the phosphorylation of peptides, such as fibrinopeptide A and alpha-melanocyte stimulating hormone."xsd:string
http://purl.uniprot.org/citations/6952938http://purl.org/dc/terms/identifier"doi:10.1016/0167-4838(82)90498-8"xsd:string
http://purl.uniprot.org/citations/6952938http://purl.uniprot.org/core/author"Farrell H.M. Jr."xsd:string
http://purl.uniprot.org/citations/6952938http://purl.uniprot.org/core/author"Szymanski E.S."xsd:string
http://purl.uniprot.org/citations/6952938http://purl.uniprot.org/core/date"1982"xsd:gYear
http://purl.uniprot.org/citations/6952938http://purl.uniprot.org/core/name"Biochim Biophys Acta"xsd:string
http://purl.uniprot.org/citations/6952938http://purl.uniprot.org/core/pages"163-172"xsd:string
http://purl.uniprot.org/citations/6952938http://purl.uniprot.org/core/title"Isolation and solubilization of casein kinase from Golgi apparatus of bovine mammary gland and phosphorylation of peptides."xsd:string
http://purl.uniprot.org/citations/6952938http://purl.uniprot.org/core/volume"702"xsd:string
http://purl.uniprot.org/citations/6952938http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/6952938
http://purl.uniprot.org/citations/6952938http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/6952938
http://purl.uniprot.org/uniprot/P67827#attribution-9FE8B0FB4A9130EE89EB06A1C433AC8Chttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/6952938
http://purl.uniprot.org/uniprot/P35507#attribution-9FE8B0FB4A9130EE89EB06A1C433AC8Chttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/6952938
http://purl.uniprot.org/uniprot/P35508#attribution-9FE8B0FB4A9130EE89EB06A1C433AC8Chttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/6952938
http://purl.uniprot.org/uniprot/Q0VC49#attribution-9FE8B0FB4A9130EE89EB06A1C433AC8Chttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/6952938
http://purl.uniprot.org/uniprot/Q32LI4#attribution-9FE8B0FB4A9130EE89EB06A1C433AC8Chttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/6952938
http://purl.uniprot.org/uniprot/A7MB68#attribution-9FE8B0FB4A9130EE89EB06A1C433AC8Chttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/6952938