ArticleJournal of bioenergetics and biomembranes2000
A quantitative approach to membrane binding of human ubiquitous mitochondrial creatine kinase using surface plasmon resonance.
Article in Journal of bioenergetics and biomembranes, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Three human aminoacyl-tRNA synthetases have distinct sub-mitochondrial localizations that are unaffected by disease-associated mutations.The Journal of biological chemistry · 2018Article
- Applications of surface plasmon resonance (SPR) for the characterization of nanoparticles developed for biomedical purposes.Sensors (Basel, Switzerland) · 2012Article
- Phosphocreatine interacts with phospholipids, affects membrane properties and exerts membrane-protective effects.PloS one · 2012Article
- Mitochondrial creatine kinase interaction with cardiolipin-containing biomimetic membranes is a two-step process involving adsorption and insertion.European biophysics journal : EBJ · 2010Article
- The nucleoside diphosphate kinase D (NM23-H4) binds the inner mitochondrial membrane with high affinity to cardiolipin and couples nucleotide transfer with respiration.The Journal of biological chemistry · 2008Article
- Novel lipid transfer property of two mitochondrial proteins that bridge the inner and outer membranes.Biophysical journal · 2007Article
- Octameric mitochondrial creatine kinase induces and stabilizes contact sites between the inner and outer membrane.The Biochemical journal · 2005Article
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Authors and funding
2 authors.
Funding
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Abstract
We have evaluated surface plasmon resonance with avidin-biotin immobilized liposomes to characterize membrane binding of ubiquitous mitochondrial creatine kinase (uMtCK). While the sarcomeric sMtCK isoform is well known to bind to negatively charged phospholipids, especially cardiolipin, this report provides the first experimental evidence on the membrane interaction of an uMtCK isoform. Qualitative measurements showed that liposomes containing 16% (w/w) cardiolipin bind octameric as well as dimeric human uMtCK and also cytochrome c, but not bovine serum albumin. Quantitative parameters could be derived only for the membrane interaction of octameric human uMtCK using an improved analytical approach. Association and dissociation kinetics of octameric uMtCK fit well to a model for heterogeneous interaction suggesting two independent binding sites. Rate constants of the two sites differed by one order of magnitude, while their affinity constants were both about 80-100 nM. The data obtained demonstrate that surface plasmon resonance with immobilized liposomes is a suitable approach to characterize the binding of peripheral proteins to a lipid bilayer and that this method yields consistent quantitative binding parameters.
Indexed as
Identifiers
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.