Modulation of mitochondrial F0F1 catalysis by boundary and bulk phase phospholipids.
The importance of boundary and bulk phase phospholipids was studied on a mitochondrial ATPase complex isolated by AH-Sepharose chromatography as described by Dreyfus et al (1984, Anal. Biochem. 142,215-220), this preparation was devoid of the adenine nucleotide carrier. The presence of isoelectric or acidic phospholipids during the purification in the column allows the exchange of tightly bound phospholipids up to 95%. ATP hydrolysis and oligomycin sensitivity were slightly affected by the nature of boundary and bulk phase phospholipids, while Pi-ATP exchange was highly inhibited.
Dabbeni-Sala
F
F
Dipartimento di Farmacologia dell'Universita di Padova, Italy.
Vázquez-Laslop
N
N
Fachinetti
A
A
Devars
S
S
Dreyfus
G
G
D000255:Adenosine Triphosphate / Q000378:metabolism; D002384:Catalysis; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D008928:Mitochondria / Q000201:enzymology*; D009840:Oligomycins / Q000494:pharmacology; D010710:Phosphates / Q000378:metabolism; D010713:Phosphatidylcholines / Q000494:pharmacology; D010743:Phospholipids / Q000494:pharmacology*; D006180:Proton-Translocating ATPases / Q000302:isolation & purification / Q000378:metabolism; D013367:Submitochondrial Particles / Q000201:enzymology
D009840:Oligomycins; D010710:Phosphates; D010713:Phosphatidylcholines; D010743:Phospholipids; C024990:asolectin; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases