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The in vitro modification of phosphorylated pyruvate kinase by a Ca2+-activated protease from rat liver
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical and Physiological Chemistry. (Engström Lorentz)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical and Physiological Chemistry. (Engström Lorentz)
1980 (English)In: Acta Chemica Scandinavica, ISSN 0904-213X, E-ISSN 1902-3103, Vol. 34, no 6, 419-422 p.Article in journal (Refereed) Published
Abstract [en]

A Ca/+-activated protease from rat liver cell sap was prepared. It was shown to act on rat liver pyruvate kinase that had been phosphorylated by the catalytic subunit of cyclic AMP-dependent protein kinase, the activity being optimum at neutral pH. The modified pyruvate kinase had the same Vmax as the phosphoenzyme but showed a lower affinity for the substrate phosphoenolpyruvate. The possibility that this proteolytic attack is the step that initiates further degradation in the cell is discussed.

Place, publisher, year, edition, pages
1980. Vol. 34, no 6, 419-422 p.
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Other Medical Sciences not elsewhere specified
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URN: urn:nbn:se:uu:diva-169297PubMedID: 7008473OAI: oai:DiVA.org:uu-169297DiVA: diva2:506090
Available from: 2012-02-27 Created: 2012-02-27 Last updated: 2017-12-07Bibliographically approved

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