Journal: PLoS ONE

Article Title: ATP hydrolytic activity of purified Spf1p correlate with micellar lipid fluidity and is dependent on conserved residues in transmembrane helix M1

doi: 10.1371/journal.pone.0274908

Figure Lengend Snippet: Specific activities reported in nmol/min/mg for purified and lipid/detergent reactivated Spf1p with the conditions for individual experiments shown. Star indicate activity measurements using radiolabeled ATP 32 , C12E10: Polyoxyethylene(10)dodecyl Ether, OG: n-Octyl-β-D-Glucopyranoside, PC/POPC: phosphatidylcholine and n.r.: not reported. For comparison polyamine stimulated activity of lipid activated ATP13A2 is ~150 nmol/min/mg [ 2 ] and for Ypk9p ~1.000 nmol/min/mg [ 18 ] both at 37⁰C, phosphatidylserine stimulated activity of the lipid flippase ATP8A1 is ~100.000 nmol/min/mg at 37⁰C [ 36 ], the activated state of the Pma1p H + ATPase is reported at ~12.000 nmol/min/mg at 30⁰C [ 37 ] and activity for SERCA and SPCA Ca 2+ ATPases are reported at ~12.000 nmol/min/mg and ~2500 nmol/min/mg respectively in proteoliposomes [ 38 ].

Article Snippet: Yeast polar lipid extracts (Avanti 190001) were dissolved in chloroform from the vial provided by the manufacturer and 1mg fractions were aliquoted into glass vials and stored at -200C under N 2 .

Techniques: Purification, Activity Assay, Comparison