Molecular and Cellular Biochemistry

, Volume 15, Issue 2, pp 145–148 | Cite as

Kinetic properties of soluble adenosine triphosphatase of escherichia coli

  • Jan Ahlers
Review and General Articles b. general articles

Summary

Bound and solubilized ATPase from Escherichia coli show similar kinetic properties. The saturation curves for MgATP are hyperbolic with both preparations. The straight lines in the Line-weaver–Burk plot indicate that MgATP is the true substrate, that one molecule MgATP is bound per enzyme molecule, and that there is no cooperativity. Presence of EDTA leads to sigmoidal saturation curves. This effect could be reversed by adding MgCl2 stoichiometrically to EDTA.

Different results in other publications, especially in that ofCarreira andMuñoz can be explained as being primarily the consequence of complexing agent contaminations in the assay.

Keywords

Escherichia Coli EDTA Adenosine MgCl2 Kinetic Property 

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Copyright information

© Dr. W. Junk b.v. Publishers 1977

Authors and Affiliations

  • Jan Ahlers
    • 1
  1. 1.Zentralinstitut für Biochemie und BiophysikFreie Universität Berlin1 BerlinGermany

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