Autophosphorylation and Autoactivation of an S6/H4 Kinase Isolated From Human Placenta

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A number of protein kinases have been shown to undergo autophosphorylation, but few have demonstrated a coordinate increase or decrease in enzymatic activity as a result. Described here is a novel S6 kinase isolated from human placenta which autoactivates through autophosphorylation in vitro. This S6/H4 kinase, purified in an inactive state, was shown to be a protein of Mr of 60,000 as estimated by SDS-PAGE and could catalyze the phosphorylation of the synthetic peptide S6-21, the histone H4, and myelin basic protein. Mild digestion of the inactive S6/H4 kinase with trypsin was necessary, but not sufficient, to activate the kinase ... continued below

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viii, 134 leaves: ill.

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Dennis, Patrick B. (Patrick Brian) May 1994.

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  • Dennis, Patrick B. (Patrick Brian)

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A number of protein kinases have been shown to undergo autophosphorylation, but few have demonstrated a coordinate increase or decrease in enzymatic activity as a result. Described here is a novel S6 kinase isolated from human placenta which autoactivates through autophosphorylation in vitro. This S6/H4 kinase, purified in an inactive state, was shown to be a protein of Mr of 60,000 as estimated by SDS-PAGE and could catalyze the phosphorylation of the synthetic peptide S6-21, the histone H4, and myelin basic protein. Mild digestion of the inactive S6/H4 kinase with trypsin was necessary, but not sufficient, to activate the kinase fully

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viii, 134 leaves: ill.

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  • May 1994

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  • March 26, 2014, 9:30 a.m.

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  • Dec. 11, 2014, 1:22 p.m.

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Dennis, Patrick B. (Patrick Brian). Autophosphorylation and Autoactivation of an S6/H4 Kinase Isolated From Human Placenta, dissertation, May 1994; Denton, Texas. (digital.library.unt.edu/ark:/67531/metadc279364/: accessed August 14, 2018), University of North Texas Libraries, Digital Library, digital.library.unt.edu; .