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Purification of a C...
Purification of a Ca2+-activated protease from rat erythrocytes and its possible effect on pyruvate kinase in vivo
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- Dahlqvist-Edberg, Ulla (author)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi,Engström Lorentz
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- Ek, Pia (author)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi,Engström Lorentz
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(creator_code:org_t)
- Elsevier BV, 1981
- 1981
- English.
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In: Biochimica et Biophysica Acta-Enzymology. - : Elsevier BV. - 0005-2744. ; 660:1, s. 96-101
- Related links:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
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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.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Annan medicin och hälsovetenskap -- Övrig annan medicin och hälsovetenskap (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Other Medical and Health Sciences -- Other Medical and Health Sciences not elsewhere specified (hsv//eng)
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- art (subject category)
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