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dc.contributor.authorPicking, William D.
dc.contributor.authorHackstadt, T.
dc.contributor.authorParetsky, D.
dc.date.accessioned2016-08-15T16:35:36Z
dc.date.available2016-08-15T16:35:36Z
dc.date.issued1989-12
dc.identifier.citationPicking, W. D., Hackstadt, T., & Paretsky, D. (1989). Endotoxicosis induced by Coxiella burnetii lipopolysaccharide stimulates a ribosomal protein S6 kinase: some properties of the partially purified enzyme. Infection and Immunity, 57(12), 3683–3688.en_US
dc.identifier.urihttp://hdl.handle.net/1808/21321
dc.description.abstractGuinea pig endotoxicosis induced by lipopolysaccharide from Coxiella burnetii Nine Mile phase I stimulates phosphorylation of liver ribosomal protein S6, with a 50% increase at 12 h postinoculation. The responsible protein kinase (S6PK) has been partially purified from liver; its activity is independent of cyclic AMP and of Ca2+ plus phosphatidyl serine or diacylglycerol. The preparation has an apparent optimum concentration of 20 mM Mg2+, while Ca2+ and Mn2+ are each inhibitory at 2 mM. The apparent Km for ATP is 30 microM with intact ribosomes. Because of the central role of phosphorylation in metabolic regulation and a purported role of phosphorylated S6 in protein synthesis, the lipopolysaccharide-induced stimulation of S6PK suggests a significant regulatory role of such enzymes in the pathobiochemistry of Q fever infection and endotoxicosis.en_US
dc.publisherAmerican Society for Microbiologyen_US
dc.relation.isversionofhttp://iai.asm.org/content/57/12/3683.longen_US
dc.titleEndotoxicosis Induced by Coxiella burnetii Lipopolysaccharide Stimulates a Ribosomal Protein S6 Kinase: Some Properties of the Partially Purified Enzymeen_US
dc.typeArticleen_US
kusw.kuauthorPicking, William D.
kusw.kudepartmentPharmaceutical Chemistryen_US
kusw.oaversionScholarly/refereed, publisher versionen_US
kusw.oapolicyThis item does not meet KU Open Access policy criteria.en_US
dc.rights.accessrightsopenAccess


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