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
| Identifer | oai:union.ndltd.org:unt.edu/info:ark/67531/metadc279364 |
| Date | 05 1900 |
| Creators | Dennis, Patrick B. (Patrick Brian) |
| Contributors | Masaracchia, Ruthann A., Wu, Edward Ming-chi, 1938-, Easom, Richard, Donahue, Manus J., Kelly, Kimberly, Pirtle, Robert M. |
| Publisher | University of North Texas |
| Source Sets | University of North Texas |
| Language | English |
| Detected Language | English |
| Type | Thesis or Dissertation |
| Format | viii, 134 leaves: ill., Text |
| Rights | Public, Copyright, Copyright is held by the author, unless otherwise noted. All rights reserved., Dennis, Patrick B. (Patrick Brian) |
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