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- W778840434 abstract "Adenosine-5'-triphosphatase in the Lentinus edodes was fractionated by ammonium aulfate 30% saturation and purified by Sephadex G-200 gel filtration in three times. Three kinds of protein fractions of were isolated from this mushroom, and fraction I and ll showed its activity for the substrate, adenosine-5'-triphosphate. Its optimum pH and temperature were found to be pH 7.6 and , and its thermal stability was stabled for 30 min. at . The Km value of this enzyme was 1.81 mM." @default.
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- W778840434 date "1991-01-01" @default.
- W778840434 modified "2023-09-28" @default.
- W778840434 title "Studies on the Adenosinetriphosphatase in the Mushroom (I) -Purification and Properties of $F_{1}-ATPase$ in Lentinus edodes (Berk.) Sing-" @default.
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