title: Interaction of caldesmon with phospholipids.
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.
authors: Department of Muscle Biochemistry, Nencki Institute of Experimental Biology, Warsaw, Poland.
authors: E A
authors: EA
authors: Czuryło
authors: J
authors: J
authors: Zborowski
authors: R
authors: R
authors: Dabrowska
mesh_terms: D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D002147:Calmodulin / Q000378:metabolism; D002148:Calmodulin-Binding Proteins / Q000378:metabolism*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002645:Chickens; D004563:Electrochemistry; D005895:Gizzard, Avian / Q000737:chemistry; D008081:Liposomes / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism; D010718:Phosphatidylserines / Q000378:metabolism; D010743:Phospholipids / Q000378:metabolism*; D012965:Sodium Chloride / Q000494:pharmacology; D013050:Spectrometry, Fluorescence
chemical_list: D002147:Calmodulin; D002148:Calmodulin-Binding Proteins; D008081:Liposomes; D010446:Peptide Fragments; D010718:Phosphatidylserines; D010743:Phospholipids; D012965:Sodium Chloride