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- E-ISSN 2288-8985
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Characteristics of <TEX>$G_{418}$</TEX>-sensitive mitochondrial ATPase/ATP synthase from pleurotus florida
Analytical Science and Technology / Analytical Science and Technology, (P)1225-0163; (E)2288-8985
1992, v.5 no.4, pp.477-484
Kim,
J., Kim,
D., Lee,
J., Lee,
S., &
Min,
T.
(1992). Characteristics of <TEX>$G_{418}$</TEX>-sensitive mitochondrial ATPase/ATP synthase from pleurotus florida. Analytical Science and Technology, 5(4), 477-484.
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Abstract
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, <TEX>$60^{\circ}C$</TEX> and pH 7.5, <TEX>$57^{\circ}C$</TEX> 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 <TEX>$Mg^{2+}$</TEX>-dependent enzyme, partially inhibited by their substrate, and then showed an none competitive inhibition pattern by <TEX>$G_{418}$</TEX>. 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(<TEX>$C_{18:1}$</TEX>, <TEX>$C_{18:2}$</TEX> and <TEX>$C_{16:1}$</TEX>) were predominated.
- keywords
- ATPase, ATP synthase, pleurotus florida
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