Interaction of rabbit muscle aldolase with phospholipid liposomes.
The interaction between rabbit muscle fructose diphosphate aldolase and phospholipid model membranes (liposomes) was studied by measurement of the tryptophan fluorescence of the enzyme. Interaction with liposomes decreases intrinsic fluorescence intensity of the enzyme and shifts the emission wavelength maximum to higher values. The effects appear to be strongly dependent on the nature of the phospholipid polar group and on ionic strength. Also, a reversible modification of specific activity of aldolase upon interaction with liposomes was found. It is postulated that aldolase binds to liposomes mainly by electrostatic interactions and that the binding causes a change in the conformation of the enzyme.
D000818:Animals; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism; D007700:Kinetics; D008081:Liposomes; D009132:Muscles / Q000201:enzymology; D009994:Osmolar Concentration; D010743:Phospholipids; D011487:Protein Conformation; D011817:Rabbits; D013050:Spectrometry, Fluorescence; D014364:Tryptophan
D008081:Liposomes; D010743:Phospholipids; D014364:Tryptophan; D005634:Fructose-Bisphosphate Aldolase