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PubMed · 8484721

Interaction of caldesmon with phospholipids.

E A Czuryło·J Zborowski·R Dabrowska
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Abstract

The interaction of caldesmon with liposomes composed of various phospholipids has been examined by tryptophan fluorescence spectroscopy. The results indicate that caldesmon makes its strongest complex with phosphatidylserine (PS) vesicles (Kass. = 1.45 x 10(5) M-1). Both electrostatic and hydrophobic interactions contribute to the stability of this complex. The site for strong binding of PS seems to be located in the N-terminal part of the 34 kDa C-terminal fragment of caldesmon. Binding of PS at this site results in displacement of calmodulin from its complex with caldesmon.

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AnimalsBinding SitesBinding, CompetitiveCalmodulinCalmodulin-Binding ProteinsChemical PhenomenaChemistry, PhysicalChickensElectrochemistryGizzard, AvianLiposomesPeptide FragmentsPhosphatidylserinesPhospholipidsSodium ChlorideSpectrometry, FluorescenceJournal Article

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E A Czuryło, J Zborowski, R Dabrowska. 1993-04-15. Interaction of caldesmon with phospholipids.. https://doi.org/10.1042/bj2910403

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