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- Dahlqvist-Edberg, UllaUppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi,Engström Lorentz (author)
Purification of a Ca2+-activated protease from rat erythrocytes and its possible effect on pyruvate kinase in vivo
- Article/chapterEnglish1981
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- Elsevier BV,1981
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- LIBRIS-ID:oai:DiVA.org:uu-169299
- https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-169299URI
- https://doi.org/10.1016/0005-2744(81)90113-3DOI
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- Language:English
- Summary in:English
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- 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.
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- Ek, PiaUppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi,Engström Lorentz(Swepub:uu)pek21046 (author)
- Uppsala universitetInstitutionen för medicinsk biokemi och mikrobiologi (creator_code:org_t)
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- In:Biochimica et Biophysica Acta-Enzymology: Elsevier BV660:1, s. 96-1010005-2744
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