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Updated: Feb 11, 2026

Scalable Isolation and Purification of Extracellular Vesicles from Escherichia coli and Other Bacteria
Published on: October 13, 2021
Ca2+ stabilization of respiratory complex I from Escherichia coli
Galina Belevich1, Nikolai Belevich1, Juho Knuuti1
1Institute of Biotechnology, University of Helsinki, PO Box 65, Helsinki FIN-00014, Finland.
Abstract:
Stability of the membrane-bound and purified H+-translocating NADH:ubiquinone oxidoreductase, Complex I, was studied. The loss of the enzyme activity is strongly increased by alkaline pH and dilution of the sample. Complex I inactivation is prevented specifically by a low concentration of Ca2+ and/or an intracellular stabilization factor (ISF). The action of both, Ca2+ and ISF, on Complex I stability is interdependent. The data are discussed in terms of a release of structural Ca2+ as a reason for Complex I decay and an effect of ISF on the affinity and/or accessibility of Ca2+-binding site.
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