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- W2352188208 abstract "The RubisCO (E. C. 4. 1. 1. 39)from Chlorella protothecoides was purified(Table 1 and Fig. 3) by ammoniumsulfate fractionation and column chromatography on Sephacryl S-300 (Fig.1) and DEAE-cellulose (Fig. 2). The recovery was 15 %. The specific activity of the enzyme was 1. 232 μmol CO2 mg-1 protein min-1. Its molecular weight was 500 kD. The molecular weight, subunit constitution (Fig. 4)and immunoreactivity (Fig. 5) of the enzyme were similar to those from spinach leaves.The content of RubisCO in totalsoluble protein in autotrophic C. protothecoides cells was 24%. No RubisCO was found in heterotrophic C. protothecoides cells (Table 2 ). RubisCO appeared in the C. protothecoides cells 24 hafter transition from heterotrophy to autotrophy. Then it kept increasing until 41 h. Chlorophyll appeared 20 h after transition from heterotrophy to autotrophy(Fig. 6, 7)." @default.
- W2352188208 created "2016-06-24" @default.
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- W2352188208 date "1994-01-01" @default.
- W2352188208 modified "2023-09-27" @default.
- W2352188208 title "Purification of RubisCO from Chlorella Chlorella protothecoides and Its Content Change During Transition fromHetertrophy to Autotrophy" @default.
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