Interaction of cytoplasmic L-glycerol-3-phosphate dehydrogenase with liposomes.
NAD-linked L-glycerol-3-phosphate dehydrogenase binds to phosphatidylcholine liposomes as shown by the changes in the properties of both the enzyme and the membrane. The surface potential and the fluidity of the liposome membrane (monitored at the 5th C atom depth) change due to the presence of the enzyme, whereas the enzyme is activated by the liposomes. These findings suggest the occurrence of peripheral protein-lipid interactions.
D000818:Animals; D003593:Cytoplasm / Q000201:enzymology; D004578:Electron Spin Resonance Spectroscopy; D005993:Glycerolphosphate Dehydrogenase / Q000378:metabolism; D007700:Kinetics; D008081:Liposomes; D010713:Phosphatidylcholines; D011485:Protein Binding; D011487:Protein Conformation; D011817:Rabbits; D013329:Structure-Activity Relationship
D008081:Liposomes; D010713:Phosphatidylcholines; D005993:Glycerolphosphate Dehydrogenase