Interactions of parvalbumins with model phospholipid vesicles.
Interactions of Ca2+-binding proteins, parvalbumins, with model vesicles formed with both synthetic (dipalmitoylphosphatidylcholine) and natural (phosphatidylcholine and phosphatidylethanolamine) phospholipids have been revealed and studied by means of gel-chromatography, electron microscopy, intrinsic fluorescence and microcalorimetry methods. There are at least two populations of liposome-bound parvalbumin one of which has higher affinity to the liposomes (effective binding constant about 10(6) M-1) than the other one. The interaction is modulated by Ca2+ and Mg2+ ions and induces changes in properties of both parvalbumin and liposomes.
Permyakov
E A
EA
Institute of Biological Physics, U.S.S.R. Academy of Sciences, Pushchino, Moscow.
Kreimer
D I
DI
Kalinichenko
L P
LP
Orlova
A A
AA
Shnyrov
V L
VL
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002151:Calorimetry / Q000379:methods; D002462:Cell Membrane / Q000378:metabolism / Q000648:ultrastructure; D002850:Chromatography, Gel; D005399:Fishes; D008081:Liposomes / Q000378:metabolism*; D008345:Manganese / Q000494:pharmacology; D008832:Microchemistry; D008854:Microscopy, Electron; D008954:Models, Biological; D009124:Muscle Proteins / Q000378:metabolism*; D010320:Parvalbumins / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism*; D013050:Spectrometry, Fluorescence
D008081:Liposomes; D009124:Muscle Proteins; D010320:Parvalbumins; D010743:Phospholipids; D008345:Manganese; D002118:Calcium