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Purification of a Ca2+-activated protease from rat erythrocytes and its possible effect on pyruvate kinase in vivo
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology. (Engström Lorentz)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology. (Engström Lorentz)
1981 (English)In: Biochimica et Biophysica Acta-Enzymology, ISSN 0005-2744, Vol. 660, no 1, 96-101 p.Article in journal (Refereed) Published
Abstract [en]

A Ca2+-activated protease with [32P]phosphopyruvate kinase as substrate was purified to about 50% from rat erythrocytes. The purification involved chromatography on Sepharose/Sephadex gels, DEAE-cellulose and (NH4)2SO4 precipitation. The protease required 3.3 mM Ca2+ for full activity. When pyruvate kinase (ATP: pyruvate 2-O-phosphotransferase, EC 2.7.1.40) was purified from erythrocytes incubated with [32P]phosphate it contained 0.5 mol [32P]phosphate/mol enzyme subunit. When 3.3 mM Ca2+ were added at hemolysis this incorporation decreased. The possible importance of this Ca2+-activated protease for the regulation of pyruvate kinase in erythrocytes is discussed.

Place, publisher, year, edition, pages
1981. Vol. 660, no 1, 96-101 p.
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Other Medical Sciences not elsewhere specified
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URN: urn:nbn:se:uu:diva-169299DOI: 10.1016/0005-2744(81)90113-3PubMedID: 6268175OAI: oai:DiVA.org:uu-169299DiVA: diva2:506091
Available from: 2012-02-27 Created: 2012-02-27 Last updated: 2012-02-27Bibliographically approved

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