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- W2280255588 abstract "The crystals of ribulose bisphosphate carboxylase were obtained through extraction with sodium metabisulfite solution at pH 6.0, heating, centrifugation and adjusting pH to 5.0, etc. The stable recrystals could be prepared by dialysis against neutral Tris buffer. SDS-gel electrophoresis showed that such recrystals were pure ribulose bisphosphate carboxylase. The specific activity of this enzyme was about 0.5 μmol mg~(-1) min~(-1) The yield of enzyme was about 7 mg g~(-1) leaf fresh weight, higher than that prepared with routine methods. The purified enzyme was dissociated with Tris buffer (pH 8.0) containing 3.5 mol/L urea, then the pH of enzyme was adjusted to 5.0 for precipitating the large subunits. The precipitate was suspended with Tris buffer containing 3.5 mol/L urea. After repeated precipitation the pure large subunits were obtained. The supernatant was dialysed against Tris buffer at pH 7.4 to precipitate the undissociated holoenzyme. It was found that the obtained supernatant was pure small subunit after centrifugation. The procedure presented here was simple, with high recovery, and is applicable to the large-scale preparation of ribulose bisphosphate carboxylase and its subunits." @default.
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- W2280255588 date "1990-01-01" @default.
- W2280255588 modified "2023-09-27" @default.
- W2280255588 title "An improved procedure for purification of ribulose-bisphosphate carboxylase and its large and small subunits from tobacco leaves." @default.
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