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Download PDF by Gerald Litwack (Eds.): Biochemical Actions of Hormones. Volume 6

By Gerald Litwack (Eds.)

ISBN-10: 0124528066

ISBN-13: 9780124528062

ISBN-10: 0323146384

ISBN-13: 9780323146388

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Dose-response relationships for 8-hydroxy-cAMP effects on induction of tyrosine aminotransferase and the phosphorylation of histone fi at the site specific for cAMP-dependent protein kinase in intact H35 cells. The analog was added at the concentrations indicated for 2 hours. Each value for histone phosphorylation represents two observations at 5μΜ, four at 50 μ,Μ, and one at 500 μ,Μ. 8-fold more than the control. Tyrosine aminotransferase (TAT) activity was determined in separate experiments 3 hours after analog addition.

Walsh and Ronald H. Cooper FRACTION NUMBER FIG. 36. The sucrose gradient sedimentation profiles of the macromolecular binding frac­ tions prelabeled by perfusion with [3H]Bt2-cAMP: Effect of the addition of the catalytic subunit of cAMP-dependent protein kinase. 32 μ,Μ [3H]Bt2-cAMP, and cytoplasmic macromolecular fractions were prepared from unfrozen tissue. 8 with the following: ( · ) , no additions; (O), 18 /i,g of pure skeletal muscle cAMP-dependent protein kinase catalytic subunit; (A), 18 /xg of catalytic subunit 5 mM magnesium chloride and 1 mM ATP.

Thus, no studies are pursued to examine the state of allosteric activation in vivo from subsequent in vitro type assays. For the protein kinase, however, conditions have been sought that would "freeze" the association-dissociation state of the enzyme during extraction. Subsequent assay of extracts, assuming that the associationdissociation state had been stabilized, could, by measuring the degree of 1. cAMP-Dependent Protein Kinases 25 cAMP dependence, reflect the amount of holoenzyme and the amount of free catalytic subunit.

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Biochemical Actions of Hormones. Volume 6 by Gerald Litwack (Eds.)

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