Use of Swinbourne plots to study potential suicide substrates: effects of ATP and ADP on yeast mitochondrial F1-ATPase.
A simple analytical procedure for comparing the rates of inactivation of an enzyme in the presence and absence of its substrate is proposed. The rapid inactivation of yeast F1-ATPase during the catalytic reaction was found to be due to certain anions rather than due to ATP or ADP. MgATP failed to protect the enzyme but substituting sulfate, acetate, bicarbonate, or N-tris(hydroxymethyl)methyl-2-aminoethane sulfonate anions and preincubation with ADP prevented the inactivation.
Jenkins
W T
WT
D000244:Adenosine Diphosphate / Q000494:pharmacology*; D000255:Adenosine Triphosphate / Q000494:pharmacology*; D007700:Kinetics; D008928:Mitochondria / Q000201:enzymology*; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases