Purification of a Ca2+-activated protease from rat erythrocytes and its possible effect on pyruvate kinase in vivo
1981 (English)In: Biochimica et Biophysica Acta-Enzymology, ISSN 0005-2744, Vol. 660, no 1, 96-101 p.Article in journal (Refereed) Published
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 126.96.36.199) 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.
Other Medical Sciences not elsewhere specified
IdentifiersURN: urn:nbn:se:uu:diva-169299DOI: 10.1016/0005-2744(81)90113-3PubMedID: 6268175OAI: oai:DiVA.org:uu-169299DiVA: diva2:506091