Tissue specificity of mitochondrial F0F1-ATPase activity of Lilium longiflorum plant.
A large difference was found in the activities of oligomycin-sensitive mitochondrial F0F1-ATPase isolated from different tissues of Lilium longiflorum plants. The enzyme activity of F0F1-ATPase in pollen was the highest, while that in bulbs was the lowest. When ATPases were cross-reconstituted from F1-ATPases and F1-depleted submitochondrial particles (SMP), ATPases reconstituted from F1-depleted pollen SMP showed the higher activity regardless of the source of F1-ATPase. Fatty acid compositions of phospholipids in SMP were also different between bulbs and pollen. These suggest that the F0 portion and/or its environment are important for regulation of F0F1-ATPase activity in L. longiflorum plant.
Itoh
A
A
Department of Agricultural Chemistry, Faculty of Agriculture, Kyoto University, Japan.
Sekiya
J
J
D004797:Enzyme-Linked Immunosorbent Assay; D007700:Kinetics; D008928:Mitochondria / Q000201:enzymology*; D009840:Oligomycins / Q000494:pharmacology; D018515:Plant Leaves; D018517:Plant Roots; D010944:Plants / Q000201:enzymology*; D011058:Pollen; D006180:Proton-Translocating ATPases / Q000302:isolation & purification / Q000378:metabolism*; D013367:Submitochondrial Particles / Q000201:enzymology
D009840:Oligomycins; D006180:Proton-Translocating ATPases