In vivo phosphorylation of phosphofructokinase at a novel site Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/rx913t55r

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  • This thesis examines the interconnection between the in vitro and in vivo phosphorylation of rabbit muscle phosphofructokinase. The first goal of the project was to show whether a novel site of rabbit muscle phosphofructokinase that is subject to in vitro phosphorylation, serine 376, may also become phosphorylated in vivo. Evidence obtained through iron chelate chromatography, amino acid analysis, gas phase sequencing, ammonium sulfate reversed phase high pressure liquid chromatography (HPLC), and matrix-assisted laser desorption/ ionization time-of-flight (MALDI-TOF) spectroscopy of cyanogen bromide digests of the enzyme purified from epinephrine-stimulated rabbit hearts demonstrate the in vivo phosphorylation of serine 376. Parallel experiments with phosphofructokinase isolated from unstimulated rabbit hearts show no detectable phosphorylation of serine 376. The second part of the thesis examines the effects of alterations in experimental conditions on the in vitro phosphorylation of rabbit muscle phosphofructokinase that is catalyzed by the cAMP-dependent protein kinase (cAMP-dPK). Significant phosphorylation of serine 376 takes place in the presence of specific proteins, calmodulin-calcium and troponin C-calcium, that are known to stabilize the catalytically inactive phosphofructokinase dimer. Conditions that stabilize the catalytic activity of phosphofructokinase generally inhibit the in vitro phosphorylation reaction.
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