Characteristics of $G_{418}$-sensitive mitochondrial ATPase/ATP synthase from pleurotus florida

사철느타리버섯 중 $G_{418}$-sensitive 미토콘드리아성 ATPase/ATP synthase의 특성

  • Kim, Jae-Woong (Department of Food and Nutrition, Yuhan Junior College) ;
  • Kim, Dong-Hee (Department of Food and Nutrition, Yuhan Junior College) ;
  • Lee, Jung-Bock (National Industrial Technology Institute) ;
  • Lee, Sur-Koo (National Industrial Technology Institute) ;
  • Min, Tae-Jin (Department of Chemistry, Dongguk University)
  • Received : 1992.12.23
  • Published : 1992.12.25


The mitochondrion was purified at 44% sucrose layer from pleurotus florida by using ultracentrifuge and sucrose density gradient method. Optimum pH and temperature of ATPase and ATP synthase were pH 7.4, $60^{\circ}C$ and pH 7.5, $57^{\circ}C$ respectively, also their Km values were determined as 11.6mM and 8.4mM. ATPase was activated at 5~6mM ATP substrate concentration, then ATP synthase was 5~10mM range ADP. ATPase/ATP synthase were $Mg^{2+}$-dependent enzyme, partially inhibited by their substrate, and then showed an none competitive inhibition pattern by $G_{418}$. Amino acid composition of ATPase/ATP synthase was as follows, hydrophobic amino acid residue was 50.5%, small residue, 56.1%, hydrogen bonding residue, 43.7% and helix breaking residue, 55.2%. Phosphatidyl choline, phosphatidyl ethanolamine and phosphatidyl glycerol were contained but not phosphatidyl inositol and phosphatidyl serine. Palmitate(51.31%), stearate(18.32%) and unsaturated fatty acids($C_{18:1}$, $C_{18:2}$ and $C_{16:1}$) were predominated.


ATPase;ATP synthase;pleurotus florida